DNM2

Summary: PMID:7590285 describes a human dynamin cDNA and proposed cell-cycle kinase motifs, but the accessible abstract does not establish a DNM2-performed step in the G2/M transition.

Reason: PMID:7590285 describes a human dynamin cDNA and proposed cell-cycle kinase motifs, but the accessible abstract does not establish a DNM2-performed step in the G2/M transition. Later PMID:21195118 directly supports mitotic phosphorylation and a cytokinesis context, which is not equivalent to this transition. Without the original operative evidence for this NAS claim, retain the source and leave this process unresolved.

Summary: The cited Reactome event places DNM2 in Golgi-associated membrane-remodeling machinery.

Reason: The cited Reactome event places DNM2 in Golgi-associated membrane-remodeling machinery. Current HPA localization independently identifies a Golgi pool, and PMID:18923138 reports splice-dependent Golgi export in a knockout/reconstitution model. Retain this trafficking context without treating every DNM2 product as constitutively Golgi-localized or adding a separate catalytic unit.

Summary: The cited Reactome event places DNM2 in Golgi-associated membrane-remodeling machinery.

Reason: The cited Reactome event places DNM2 in Golgi-associated membrane-remodeling machinery. Current HPA localization independently identifies a Golgi pool, and PMID:18923138 reports splice-dependent Golgi export in a knockout/reconstitution model. Retain this trafficking context without treating every DNM2 product as constitutively Golgi-localized or adding a separate catalytic unit.

Summary: The cited Reactome event places DNM2 in Golgi-associated membrane-remodeling machinery.

Reason: The cited Reactome event places DNM2 in Golgi-associated membrane-remodeling machinery. Current HPA localization independently identifies a Golgi pool, and PMID:18923138 reports splice-dependent Golgi export in a knockout/reconstitution model. Retain this trafficking context without treating every DNM2 product as constitutively Golgi-localized or adding a separate catalytic unit.

Summary: The cited Reactome event places DNM2 in Golgi-associated membrane-remodeling machinery.

Reason: The cited Reactome event places DNM2 in Golgi-associated membrane-remodeling machinery. Current HPA localization independently identifies a Golgi pool, and PMID:18923138 reports splice-dependent Golgi export in a knockout/reconstitution model. Retain this trafficking context without treating every DNM2 product as constitutively Golgi-localized or adding a separate catalytic unit.

Summary: The UniProt subcellular-location mapping identifies a phagocytic-cup context.

Reason: The UniProt subcellular-location mapping identifies a phagocytic-cup context. Dynamin-dependent engulfment and phagosome maturation are supported across model systems in PMID:18425118, but the available abstract does not resolve the particular human cup-localization experiment. Retain the curated location as a contextual pool, without inferring a distinct phagocytic activity from localization alone.

Summary: PMID:18480402 reports a dynamin-2/PSTPIP1 complex in the uropod of polarized cells.

Reason: PMID:18480402 reports a dynamin-2/PSTPIP1 complex in the uropod of polarized cells. The curated IDA is retained as a specialized cell-migration localization; the original imaging details were not independently recovered, and this does not make uropod localization a universal property of DNM2.

Summary: The UniProt uropod mapping is consistent with the independent experimental localization in PMID:18480402.

Reason: The UniProt uropod mapping is consistent with the independent experimental localization in PMID:18480402. Retain this specialized polarized-cell pool, without extending it to all tissues or products.

Summary: The UniProt mapping records a podosome pool of DNM2.

Reason: The UniProt mapping records a podosome pool of DNM2. This is compatible with its membrane and actin remodeling machinery, but does not identify a separate ubiquitous molecular activity. Retain the location as a context-dependent assertion rather than infer a new podosome process.

Summary: The literal PAINT IBD at PTN000170013 lies on the path to human DNM2; human self-evidence is legitimate descendant grounding, not circularity.

Reason: The literal PAINT IBD at PTN000170013 lies on the path to human DNM2; human self-evidence is legitimate descendant grounding, not circularity. The more informative gene-level function is GTPase motor activity: purified human DNM2 hydrolysis and membrane-fission experiments in PMIDs:24970086 and 36445308 connect the nucleotide reaction to mechanical membrane remodeling. This refinement preserves the original evidence and does not claim that each cited source independently measured human fission. Current GO is_a ancestry places GO:0061791 below GO:0003924. Public annotation queries show no motor annotation on the seven examined human dynamin-family proteins but do show PomBase use on dynamin-family proteins, including the membrane-scission child term. This is a supported specificity refinement, not a claim that every donor or original source measured the motor step.

Proposed replacements: GTPase motor activity

Summary: The source assays rat DNM2 constructs, including purified full-length and PH-domain variants; host species must not be substituted for construct species.

Reason: The source assays rat DNM2 constructs, including purified full-length and PH-domain variants; host species must not be substituted for construct species. The more informative gene-level function is GTPase motor activity: purified human DNM2 hydrolysis and membrane-fission experiments in PMIDs:24970086 and 36445308 connect the nucleotide reaction to mechanical membrane remodeling. This refinement preserves the original evidence and does not claim that each cited source independently measured human fission. Current GO is_a ancestry places GO:0061791 below GO:0003924. Public annotation queries show no motor annotation on the seven examined human dynamin-family proteins but do show PomBase use on dynamin-family proteins, including the membrane-scission child term. This is a supported specificity refinement, not a claim that every donor or original source measured the motor step.

Proposed replacements: GTPase motor activity

Summary: The InterPro/Rhea-derived catalytic mapping is compatible with the conserved dynamin GTPase domain.

Reason: The InterPro/Rhea-derived catalytic mapping is compatible with the conserved dynamin GTPase domain. The more informative gene-level function is GTPase motor activity: purified human DNM2 hydrolysis and membrane-fission experiments in PMIDs:24970086 and 36445308 connect the nucleotide reaction to mechanical membrane remodeling. This refinement preserves the original evidence and does not claim that each cited source independently measured human fission. Current GO is_a ancestry places GO:0061791 below GO:0003924. Public annotation queries show no motor annotation on the seven examined human dynamin-family proteins but do show PomBase use on dynamin-family proteins, including the membrane-scission child term. This is a supported specificity refinement, not a claim that every donor or original source measured the motor step.

Proposed replacements: GTPase motor activity

Summary: The cited Shank study describes DNM2 as a GTPase, rather than independently measuring every aspect of the catalytic cycle.

Reason: The cited Shank study describes DNM2 as a GTPase, rather than independently measuring every aspect of the catalytic cycle. The more informative gene-level function is GTPase motor activity: purified human DNM2 hydrolysis and membrane-fission experiments in PMIDs:24970086 and 36445308 connect the nucleotide reaction to mechanical membrane remodeling. This refinement preserves the original evidence and does not claim that each cited source independently measured human fission. Current GO is_a ancestry places GO:0061791 below GO:0003924. Public annotation queries show no motor annotation on the seven examined human dynamin-family proteins but do show PomBase use on dynamin-family proteins, including the membrane-scission child term. This is a supported specificity refinement, not a claim that every donor or original source measured the motor step.

Proposed replacements: GTPase motor activity

Summary: The Reactome event explicitly uses the DNM2-containing GTPase catalyst.

Reason: The Reactome event explicitly uses the DNM2-containing GTPase catalyst. The more informative gene-level function is GTPase motor activity: purified human DNM2 hydrolysis and membrane-fission experiments in PMIDs:24970086 and 36445308 connect the nucleotide reaction to mechanical membrane remodeling. This refinement preserves the original evidence and does not claim that each cited source independently measured human fission. Current GO is_a ancestry places GO:0061791 below GO:0003924. Public annotation queries show no motor annotation on the seven examined human dynamin-family proteins but do show PomBase use on dynamin-family proteins, including the membrane-scission child term. This is a supported specificity refinement, not a claim that every donor or original source measured the motor step.

Proposed replacements: GTPase motor activity

Summary: The Reactome trans-Golgi budding event assigns a DNM2-containing GTPase catalyst.

Reason: The Reactome trans-Golgi budding event assigns a DNM2-containing GTPase catalyst. The more informative gene-level function is GTPase motor activity: purified human DNM2 hydrolysis and membrane-fission experiments in PMIDs:24970086 and 36445308 connect the nucleotide reaction to mechanical membrane remodeling. This refinement preserves the original evidence and does not claim that each cited source independently measured human fission. Current GO is_a ancestry places GO:0061791 below GO:0003924. Public annotation queries show no motor annotation on the seven examined human dynamin-family proteins but do show PomBase use on dynamin-family proteins, including the membrane-scission child term. This is a supported specificity refinement, not a claim that every donor or original source measured the motor step.

Proposed replacements: GTPase motor activity

Summary: The Reactome budding reaction contains a DNM2 GTPase catalyst.

Reason: The Reactome budding reaction contains a DNM2 GTPase catalyst. The more informative gene-level function is GTPase motor activity: purified human DNM2 hydrolysis and membrane-fission experiments in PMIDs:24970086 and 36445308 connect the nucleotide reaction to mechanical membrane remodeling. This refinement preserves the original evidence and does not claim that each cited source independently measured human fission. Current GO is_a ancestry places GO:0061791 below GO:0003924. Public annotation queries show no motor annotation on the seven examined human dynamin-family proteins but do show PomBase use on dynamin-family proteins, including the membrane-scission child term. This is a supported specificity refinement, not a claim that every donor or original source measured the motor step.

Proposed replacements: GTPase motor activity

Summary: The Reactome vesicle-release reaction contains DNM2 in the GTP-dependent machinery.

Reason: The Reactome vesicle-release reaction contains DNM2 in the GTP-dependent machinery. The more informative gene-level function is GTPase motor activity: purified human DNM2 hydrolysis and membrane-fission experiments in PMIDs:24970086 and 36445308 connect the nucleotide reaction to mechanical membrane remodeling. This refinement preserves the original evidence and does not claim that each cited source independently measured human fission. Current GO is_a ancestry places GO:0061791 below GO:0003924. Public annotation queries show no motor annotation on the seven examined human dynamin-family proteins but do show PomBase use on dynamin-family proteins, including the membrane-scission child term. This is a supported specificity refinement, not a claim that every donor or original source measured the motor step.

Proposed replacements: GTPase motor activity

Summary: PMID:11583995 reports DNM2 binding to the postsynaptic scaffold SHANK2.

Reason: PMID:11583995 reports DNM2 binding to the postsynaptic scaffold SHANK2. The recovered primary text maps a Shank/ProSAP interaction that is not simply binding the partner SH3 domain. Scaffold protein binding captures the established partner class; it does not make DNM2 itself a scaffold or establish every synaptic process. Rat brain fractionation and recombinant interaction experiments remain distinct from a universal human-neuron localization claim.

Proposed replacements: scaffold protein binding

Summary: PMID:11583995 reports DNM2 binding to the postsynaptic scaffold SHANK1.

Reason: PMID:11583995 reports DNM2 binding to the postsynaptic scaffold SHANK1. The recovered primary text maps a Shank/ProSAP interaction that is not simply binding the partner SH3 domain. Scaffold protein binding captures the established partner class; it does not make DNM2 itself a scaffold or establish every synaptic process. Rat brain fractionation and recombinant interaction experiments remain distinct from a universal human-neuron localization claim.

Proposed replacements: scaffold protein binding

Summary: PMID:15703209 directly tests SNX9 SH3/DNM2 PRD recognition with domain-deletion and GST controls, and demonstrates endogenous association in HeLa cytosolic and membrane fractions.

Reason: PMID:15703209 directly tests SNX9 SH3/DNM2 PRD recognition with domain-deletion and GST controls, and demonstrates endogenous association in HeLa cytosolic and membrane fractions. Refine to SH3 domain binding. Recombinant template species is not resolved merely from the host-cell assay; the positive human endogenous association independently grounds the pair.

Proposed replacements: SH3 domain binding

Summary: PMID:16325581 identifies the SH3 domain of SH3BP4 as the dynamin-binding region in the transferrin-trafficking machinery.

Reason: PMID:16325581 identifies the SH3 domain of SH3BP4 as the dynamin-binding region in the transferrin-trafficking machinery. The source abstract and curated interaction support SH3 domain binding, without assigning SH3BP4 adaptor activity or transferrin-receptor binding directly to DNM2.

Proposed replacements: SH3 domain binding

Summary: PMID:16551695 reports PACSIN2 SH3 interaction with the DNM2 proline-rich region.

Reason: PMID:16551695 reports PACSIN2 SH3 interaction with the DNM2 proline-rich region. This supports SH3 domain binding; Golgi-related cellular perturbations are a separate context and do not mean that DNM2 enables the partner BAR-domain activity.

Proposed replacements: SH3 domain binding

Summary: PMID:16636290 directly uses a DNM2 proline-rich peptide as a cortactin SH3-binding comparator.

Reason: PMID:16636290 directly uses a DNM2 proline-rich peptide as a cortactin SH3-binding comparator. Refine to SH3 domain binding. The unusual AMAP1 complex and its stoichiometry in the same paper must not be transferred to this DNM2 peptide experiment.

Proposed replacements: SH3 domain binding

Summary: The literal PMID:16696976 interaction record reports surface-plasmon-resonance binding between a DNM2 proline-rich fragment and the GRB2 N-terminal SH3 domain.

Reason: The literal PMID:16696976 interaction record reports surface-plasmon-resonance binding between a DNM2 proline-rich fragment and the GRB2 N-terminal SH3 domain. This supports SH3 domain binding to GRB2. The MINT record explicitly states that the protein taxids were unspecified and human homologs were used for annotation; preserve that historical construct limit rather than describe the assay as an authenticated all-human preparation.

Proposed replacements: SH3 domain binding

Summary: The literal PMID:16696976 interaction record reports surface-plasmon-resonance binding between a DNM2 proline-rich fragment and an ITSN1 fragment containing its SH3 domains.

Reason: The literal PMID:16696976 interaction record reports surface-plasmon-resonance binding between a DNM2 proline-rich fragment and an ITSN1 fragment containing its SH3 domains. This supports SH3 domain binding to ITSN1. The MINT record explicitly states that the protein taxids were unspecified and human homologs were used for annotation; preserve that historical construct limit rather than describe the assay as an authenticated all-human preparation.

Proposed replacements: SH3 domain binding

Summary: The literal PMID:16696976 interaction record reports surface-plasmon-resonance binding between a DNM2 proline-rich fragment and the endophilin-A1 SH3 domain.

Reason: The literal PMID:16696976 interaction record reports surface-plasmon-resonance binding between a DNM2 proline-rich fragment and the endophilin-A1 SH3 domain. This supports SH3 domain binding to SH3GL2. The MINT record explicitly states that the protein taxids were unspecified and human homologs were used for annotation; preserve that historical construct limit rather than describe the assay as an authenticated all-human preparation.

Proposed replacements: SH3 domain binding

Summary: PMID:17257598 tests the human MYO1E SH3 domain against overexpressed human DNM2 and endogenous DNM2, with the W1089K SH3 mutant as a binding control.

Reason: PMID:17257598 tests the human MYO1E SH3 domain against overexpressed human DNM2 and endogenous DNM2, with the W1089K SH3 mutant as a binding control. Refine to SH3 domain binding. Separate purified rat-brain dynamin and brain co-immunoprecipitation experiments are corroboration, not human purified-protein assays.

Proposed replacements: SH3 domain binding

Summary: The PMID:17257598 endophilin SH3 pull-down provides positive dynamin association in rat-brain material.

Reason: The PMID:17257598 endophilin SH3 pull-down provides positive dynamin association in rat-brain material. Independent curated DNM2/endophilin SH3 surface-plasmon-resonance evidence in PMID:16696976 supports the same binding class, with its unspecified-template-species caveat. Refine the gene-level function to SH3 domain binding without calling this particular brain experiment human.

Proposed replacements: SH3 domain binding

Summary: PMID:17412836 establishes DNM2 association with HIV-1 Nef using human-cell complexes and controlled interaction experiments.

Reason: PMID:17412836 establishes DNM2 association with HIV-1 Nef using human-cell complexes and controlled interaction experiments. The middle/GED regions rather than the proline-rich tail are important in this context. Retain positive binding as non-core; association with a viral protein does not establish an antiviral activity or a new intrinsic signaling function.

Summary: PMID:17676042 links loss of the BIN1 SH3 interaction region to defective DNM2 binding.

Reason: PMID:17676042 links loss of the BIN1 SH3 interaction region to defective DNM2 binding. Human DNM2/BIN1 SH3-PRD coupling and membrane remodeling are independently examined in PMID:36445308. Refine to SH3 domain binding while preserving the original disease-variant and construct contexts.

Proposed replacements: SH3 domain binding

Summary: PMID:18353773 supports DNM2 association with SNX33 in endocytic trafficking.

Reason: PMID:18353773 supports DNM2 association with SNX33 in endocytic trafficking. The accessible source and curated pair establish positive binding but do not independently resolve the DNM2-contacting domain or a sufficiently precise partner-class activity. Retain the interaction as non-core, without importing SNX9-specific domain experiments as proof for SNX33.

Summary: PMID:18388313 tests SNX9-dependent recruitment and its SH3 region, and the curated pull-down uses the SNX9 SH3 fragment.

Reason: PMID:18388313 tests SNX9-dependent recruitment and its SH3 region, and the curated pull-down uses the SNX9 SH3 fragment. Refine to SH3 domain binding, corroborated by the controlled SNX9/PRD assays in PMID:15703209. The historical MINT record does not establish the exact dynamin template species; COS-7 is the assay host, not proof of a human construct.

Proposed replacements: SH3 domain binding

Summary: PMID:18480402 supports a positive DNM2/PSTPIP1 complex in polarized cells.

Reason: PMID:18480402 supports a positive DNM2/PSTPIP1 complex in polarized cells. The accessible evidence does not resolve a target-specific contact domain or a separate DNM2 adaptor activity. Retain the binding as non-core, with uropod localization assessed separately.

Summary: The original source supports DNM2 association with GRB2 through tandem-affinity purification of the BCR-ABL signaling network.

Reason: The original source supports DNM2 association with GRB2 through tandem-affinity purification of the BCR-ABL signaling network. Independent domain-resolved evidence in PMID:16696976 establishes the DNM2 proline-rich-region/GRB2 SH3 interaction, so SH3 domain binding is an informative gene-level refinement. The present source itself does not map that interface or prove a physiological signaling role; the older purified assay also retains its recorded unresolved-template-species limitation.

Proposed replacements: SH3 domain binding

Summary: PMID:20711168 demonstrates DNM2 PRD binding to CIN85 SH3A/SH3C regions, with direct binding and human endogenous co-immunoprecipitation.

Reason: PMID:20711168 demonstrates DNM2 PRD binding to CIN85 SH3A/SH3C regions, with direct binding and human endogenous co-immunoprecipitation. Refine to SH3 domain binding. The late EGFR-trafficking phenotype is not evidence that this interaction is required for initial EGFR uptake.

Proposed replacements: SH3 domain binding

Summary: The original source supports DNM2 association with GRB2 through quantitative GRB2 affinity-purification/selected-reaction-monitoring in HEK293T cells.

Reason: The original source supports DNM2 association with GRB2 through quantitative GRB2 affinity-purification/selected-reaction-monitoring in HEK293T cells. Independent domain-resolved evidence in PMID:16696976 establishes the DNM2 proline-rich-region/GRB2 SH3 interaction, so SH3 domain binding is an informative gene-level refinement. The present source itself does not map that interface or prove a physiological signaling role; the older purified assay also retains its recorded unresolved-template-species limitation.

Proposed replacements: SH3 domain binding

Summary: the PMID:21900206 yeast-two-hybrid map records a positive DNM2/DNM1 association.

Reason: the PMID:21900206 yeast-two-hybrid map records a positive DNM2/DNM1 association. DNM1 is a dynamin GTPase, and PMID:22022388 independently reports a binary DNM1-DNM2 interaction. GTPase binding describes the partner class without asserting GTPase activation, identical homodimerization, or a purified direct interface in an affinity-purification experiment. OpenCell accession groups do not resolve a unique DNM1 or DNM2 isoform.

Proposed replacements: GTPase binding

Summary: The PMID:21900206 binary map supports DNM2/ITSN1 association.

Reason: The PMID:21900206 binary map supports DNM2/ITSN1 association. The domain-resolved ITSN1 SH3-fragment interaction in PMID:16696976 supports SH3 domain binding as a gene-level refinement; its template-species limitation and the distinct screen context are retained.

Proposed replacements: SH3 domain binding

Summary: The original source supports DNM2 association with GRB2 through the human liver yeast-two-hybrid map.

Reason: The original source supports DNM2 association with GRB2 through the human liver yeast-two-hybrid map. Independent domain-resolved evidence in PMID:16696976 establishes the DNM2 proline-rich-region/GRB2 SH3 interaction, so SH3 domain binding is an informative gene-level refinement. The present source itself does not map that interface or prove a physiological signaling role; the older purified assay also retains its recorded unresolved-template-species limitation.

Proposed replacements: SH3 domain binding

Summary: PMID:22022388 reports binary interaction of sequenced human DNM2 and NPRAP/CTNND2 constructs, plus cellular association.

Reason: PMID:22022388 reports binary interaction of sequenced human DNM2 and NPRAP/CTNND2 constructs, plus cellular association. CTNND2 is delta-catenin, so beta-catenin, alpha-catenin and cadherin-binding terms would misidentify the partner. Retain positive binding as non-core without inferring an adhesion or transcriptional activity of DNM2.

Summary: PMID:22623184 explicitly identifies the AHI1 SH3 domain as the DNM2-binding region; the curated fragment is residues 1048-1116.

Reason: PMID:22623184 explicitly identifies the AHI1 SH3 domain as the DNM2-binding region; the curated fragment is residues 1048-1116. Refine to SH3 domain binding. The AHI1 crystal is not a DNM2 complex, and its modeled peptide interface does not establish a DNM2 structure or kinase activity.

Proposed replacements: SH3 domain binding

Summary: PMID:24970086 directly tests purified human NME2-DNM2 association and couples NME2 nucleotide regeneration to dynamin GTPase activity.

Reason: PMID:24970086 directly tests purified human NME2-DNM2 association and couples NME2 nucleotide regeneration to dynamin GTPase activity. NME2 is a nucleoside-diphosphate kinase, so kinase binding is supported. DNM2 does not thereby acquire kinase activity, and the separate fission panels use rat-brain dynamin or DNM1.

Proposed replacements: kinase binding

Summary: The original source supports DNM2 association with GRB2 through the pooled barcode-fusion genetics interaction screen.

Reason: The original source supports DNM2 association with GRB2 through the pooled barcode-fusion genetics interaction screen. Independent domain-resolved evidence in PMID:16696976 establishes the DNM2 proline-rich-region/GRB2 SH3 interaction, so SH3 domain binding is an informative gene-level refinement. The present source itself does not map that interface or prove a physiological signaling role; the older purified assay also retains its recorded unresolved-template-species limitation.

Proposed replacements: SH3 domain binding

Summary: The source identifies positive DNM2/SNX9 association in the barcode-fusion genetics binary screen.

Reason: The source identifies positive DNM2/SNX9 association in the barcode-fusion genetics binary screen. The independent SNX9 SH3/ DNM2 PRD experiments in PMID:15703209 support SH3 domain binding. This is a gene-level refinement, not a claim that the present screen or co-purification resolves the interface; OpenCell protein groups are retained without assigning a unique splice product.

Proposed replacements: SH3 domain binding

Summary: PMID:29437695 shows SNX18 wild-type association with endogenous DNM2 in human HEK293A cells and loss with its SH3 W38K mutant.

Reason: PMID:29437695 shows SNX18 wild-type association with endogenous DNM2 in human HEK293A cells and loss with its SH3 W38K mutant. Refine to SH3 domain binding. Recycling-endosome/ATG9 trafficking and autophagy phenotypes are source-specific cellular consequences, not proof of an autonomous SNX18-like membrane-shaping activity in DNM2.

Proposed replacements: SH3 domain binding

Summary: The original source supports DNM2 association with GRB2 through FLAG-bait affinity purification in HCT116/HKE3 colorectal-cell networks.

Reason: The original source supports DNM2 association with GRB2 through FLAG-bait affinity purification in HCT116/HKE3 colorectal-cell networks. Independent domain-resolved evidence in PMID:16696976 establishes the DNM2 proline-rich-region/GRB2 SH3 interaction, so SH3 domain binding is an informative gene-level refinement. The present source itself does not map that interface or prove a physiological signaling role; the older purified assay also retains its recorded unresolved-template-species limitation.

Proposed replacements: SH3 domain binding

Summary: The HuRI records contain sequence-matched DNM2 and SDCBP positives in validated, array and pooled two-hybrid formats.

Reason: The HuRI records contain sequence-matched DNM2 and SDCBP positives in validated, array and pooled two-hybrid formats. SDCBP is an established multivalent scaffold, supporting scaffold protein binding as a partner-class refinement. This does not demonstrate DNM2 scaffold activity or a native complex in any particular tissue.

Proposed replacements: scaffold protein binding

Summary: The HuRI records establish sequence-matched binary DNM2/RNF8 interaction across the recorded screen and validation stages.

Reason: The HuRI records establish sequence-matched binary DNM2/RNF8 interaction across the recorded screen and validation stages. The assayed partner is an established ubiquitin-protein ligase, supporting ubiquitin protein ligase binding. The experiment does not show that DNM2 is ubiquitinated by that ligase or that DNM2 itself catalyzes ubiquitin transfer.

Proposed replacements: ubiquitin protein ligase binding

Summary: The HuRI DNM2/BAG3 pair is positive with matched assayed sequences.

Reason: The HuRI DNM2/BAG3 pair is positive with matched assayed sequences. The official BAG3 functional record describes its connection of HSP70 and small heat-shock proteins in chaperone assemblies, supporting scaffold protein binding as the partner class. This is not a claim that BAG3 itself folds the client, that DNM2 is a chaperone, or that this screen establishes a native DNM2 proteostasis pathway.

Proposed replacements: scaffold protein binding

Summary: The HuRI pair maps exactly to human DNM2 and QARS1.

Reason: The HuRI pair maps exactly to human DNM2 and QARS1. QARS1 is a glutaminyl-tRNA synthetase enzyme, so enzyme binding is a literal partner-class refinement. The screen does not establish aminoacylation regulation or participation of DNM2 in translation.

Proposed replacements: enzyme binding

Summary: The HuRI assayed sequences match DNM2 and PRKAA2, the serine/threonine catalytic subunit of AMPK.

Reason: The HuRI assayed sequences match DNM2 and PRKAA2, the serine/threonine catalytic subunit of AMPK. Protein serine/threonine kinase binding is supported as a partner class; no DNM2 kinase activity, phosphorylation site, or physiological AMPK regulatory mechanism is inferred.

Proposed replacements: protein serine/threonine kinase binding

Summary: The HuRI pair is with literal UBASH3A isoform P57075-2, whose sequence and retained SH3 domain were checked.

Reason: The HuRI pair is with literal UBASH3A isoform P57075-2, whose sequence and retained SH3 domain were checked. Positive whole-protein binary binding does not locate the contact to that SH3 domain, and UBASH3A is not appropriately treated as an active protein phosphatase merely from its family label. Retain non-core binding without changing the assayed accession or inventing a domain interface.

Summary: The HuRI records contain a sequence-matched DNM2/SEC23A binary interaction.

Reason: The HuRI records contain a sequence-matched DNM2/SEC23A binary interaction. SEC23A is a COPII coat component; this assay does not establish a DNM2 COPII function or identify a narrower applicable binding activity. Preserve the positive binding as non-core.

Summary: The HuRI partner is literal FLAD1 isoform Q8NFF5-2, with its 490-residue sequence independently matched to the recorded assay.

Reason: The HuRI partner is literal FLAD1 isoform Q8NFF5-2, with its 490-residue sequence independently matched to the recorded assay. This product retains the FAD-synthetase portion of the enzyme, supporting enzyme binding as a partner-class refinement. The binary screen does not establish regulation of FAD metabolism or transfer full-length FLAD1 functions to every alternative product.

Proposed replacements: enzyme binding

Summary: The HuRI records establish sequence-matched binary DNM2/TRAF4 interaction across the recorded screen and validation stages.

Reason: The HuRI records establish sequence-matched binary DNM2/TRAF4 interaction across the recorded screen and validation stages. The assayed partner is an established ubiquitin-protein ligase, supporting ubiquitin protein ligase binding. The experiment does not show that DNM2 is ubiquitinated by that ligase or that DNM2 itself catalyzes ubiquitin transfer.

Proposed replacements: ubiquitin protein ligase binding

Summary: DNM2 associates with the recorded GABARAP-family ubiquitin-like modifiers.

Reason: PMID:32315611 reports positive association with GABARAP, GABARAPL1 and GABARAPL2. Their independently curated ubiquitin-like modifier class supports GO:0032182, without transferring conjugating activity or an adaptor function to DNM2. Preserve the complete original partner list and the study-specific association evidence; the separate LC3 recruitment experiments do not establish identical affinities or mechanisms for every GABARAP paralog.

Proposed replacements: ubiquitin-like protein binding

Summary: PMID:32315611 reports increased ITSN1 association and redistribution of a disease-associated DNM2 mutant.

Reason: PMID:32315611 reports increased ITSN1 association and redistribution of a disease-associated DNM2 mutant. The independently measured ITSN1 SH3-fragment interaction in PMID:16696976 supports SH3 domain binding. This does not mean all variants lose catalysis, and the 2020 HA-DNM2 construct is rat despite its mammalian-cell host.

Proposed replacements: SH3 domain binding

Summary: DNM2 binds the ubiquitin-like modifier LC3B during recruitment to recycling endosomes.

Reason: PMID:32315611 supports DNM2–LC3B association and LC3-dependent recruitment for recycling-endosome scission. LC3B is a ubiquitin-like modifier, supporting the binding-class refinement GO:0032182. The current purified-protein catalog sequence matches human P50570-1, but the historical lot was not authenticated and the cellular HA construct is rat. This does not assign ubiquitin transfer or an adaptor activity to DNM2.

Proposed replacements: ubiquitin-like protein binding

Summary: The original source supports DNM2 association with GRB2 through the BioPlex affinity-purification network.

Reason: The original source supports DNM2 association with GRB2 through the BioPlex affinity-purification network. Independent domain-resolved evidence in PMID:16696976 establishes the DNM2 proline-rich-region/GRB2 SH3 interaction, so SH3 domain binding is an informative gene-level refinement. The present source itself does not map that interface or prove a physiological signaling role; the older purified assay also retains its recorded unresolved-template-species limitation.

Proposed replacements: SH3 domain binding

Summary: the BioPlex affinity-purification data records a positive DNM2/DNM1 association.

Reason: the BioPlex affinity-purification data records a positive DNM2/DNM1 association. DNM1 is a dynamin GTPase, and PMID:22022388 independently reports a binary DNM1-DNM2 interaction. GTPase binding describes the partner class without asserting GTPase activation, identical homodimerization, or a purified direct interface in an affinity-purification experiment. OpenCell accession groups do not resolve a unique DNM1 or DNM2 isoform.

Proposed replacements: GTPase binding

Summary: BioPlex supplies a positive DNM2/SNX33 co-complex association.

Reason: BioPlex supplies a positive DNM2/SNX33 co-complex association. The exact target edge and bait direction are retained, but this assay does not resolve a direct interface or establish the SNX33 SH3 contact by analogy to SNX9. Keep the interaction as non-core.

Summary: The source identifies positive DNM2/SNX9 association in BioPlex affinity purification.

Reason: The source identifies positive DNM2/SNX9 association in BioPlex affinity purification. The independent SNX9 SH3/ DNM2 PRD experiments in PMID:15703209 support SH3 domain binding. This is a gene-level refinement, not a claim that the present screen or co-purification resolves the interface; OpenCell protein groups are retained without assigning a unique splice product.

Proposed replacements: SH3 domain binding

Summary: reciprocal endogenous-tag OpenCell co-purifications records a positive DNM2/DNM1 association.

Reason: reciprocal endogenous-tag OpenCell co-purifications records a positive DNM2/DNM1 association. DNM1 is a dynamin GTPase, and PMID:22022388 independently reports a binary DNM1-DNM2 interaction. GTPase binding describes the partner class without asserting GTPase activation, identical homodimerization, or a purified direct interface in an affinity-purification experiment. OpenCell accession groups do not resolve a unique DNM1 or DNM2 isoform.

Proposed replacements: GTPase binding

Summary: The source identifies positive DNM2/SNX9 association in reciprocal endogenous-tag OpenCell purification.

Reason: The source identifies positive DNM2/SNX9 association in reciprocal endogenous-tag OpenCell purification. The independent SNX9 SH3/ DNM2 PRD experiments in PMID:15703209 support SH3 domain binding. This is a gene-level refinement, not a claim that the present screen or co-purification resolves the interface; OpenCell protein groups are retained without assigning a unique splice product.

Proposed replacements: SH3 domain binding

Summary: The original source supports DNM2 association with GRB2 through the U2OS affinity-purification network.

Reason: The original source supports DNM2 association with GRB2 through the U2OS affinity-purification network. Independent domain-resolved evidence in PMID:16696976 establishes the DNM2 proline-rich-region/GRB2 SH3 interaction, so SH3 domain binding is an informative gene-level refinement. The present source itself does not map that interface or prove a physiological signaling role; the older purified assay also retains its recorded unresolved-template-species limitation.

Proposed replacements: SH3 domain binding

Summary: the U2OS affinity-purification data records a positive DNM2/DNM1 association.

Reason: the U2OS affinity-purification data records a positive DNM2/DNM1 association. DNM1 is a dynamin GTPase, and PMID:22022388 independently reports a binary DNM1-DNM2 interaction. GTPase binding describes the partner class without asserting GTPase activation, identical homodimerization, or a purified direct interface in an affinity-purification experiment. OpenCell accession groups do not resolve a unique DNM1 or DNM2 isoform.

Proposed replacements: GTPase binding

Summary: The U2OS AP-MS source records DNM2-bait association with ITSN1.

Reason: The U2OS AP-MS source records DNM2-bait association with ITSN1. Independent ITSN1 SH3-fragment binding in PMID:16696976 supports SH3 domain binding as a gene-level refinement. The network edge itself is a co-complex observation, not a mapped direct interface, and the older purified-assay template-species uncertainty remains explicit.

Proposed replacements: SH3 domain binding

Summary: the U2OS AP-MS network supplies a positive DNM2/SNX33 co-complex association.

Reason: the U2OS AP-MS network supplies a positive DNM2/SNX33 co-complex association. The exact target edge and bait direction are retained, but this assay does not resolve a direct interface or establish the SNX33 SH3 contact by analogy to SNX9. Keep the interaction as non-core.

Summary: The source identifies positive DNM2/SNX9 association in the U2OS affinity-purification network.

Reason: The source identifies positive DNM2/SNX9 association in the U2OS affinity-purification network. The independent SNX9 SH3/ DNM2 PRD experiments in PMID:15703209 support SH3 domain binding. This is a gene-level refinement, not a claim that the present screen or co-purification resolves the interface; OpenCell protein groups are retained without assigning a unique splice product.

Proposed replacements: SH3 domain binding

Summary: GTP binding is an established property of the dynamin catalytic domain and is required for the coupled motor cycle.

Reason: GTP binding is an established property of the dynamin catalytic domain and is required for the coupled motor cycle. Retain this molecular prerequisite as non-core rather than represent nucleotide occupancy as a second independent function.

Summary: GTP binding is an established property of the dynamin catalytic domain and is required for the coupled motor cycle.

Reason: GTP binding is an established property of the dynamin catalytic domain and is required for the coupled motor cycle. Retain this molecular prerequisite as non-core rather than represent nucleotide occupancy as a second independent function.

Summary: PMID:34744632 directly assays lipid binding of rat DNM2 and PH-domain constructs, with distinct effects of the tested disease variants.

Reason: PMID:34744632 directly assays lipid binding of rat DNM2 and PH-domain constructs, with distinct effects of the tested disease variants. PIP2 recognition is an integral membrane-recruitment mechanism of the motor, not a second autonomous catalytic unit. The source construct species and the absence of an all-splice-product comparison are retained.

Summary: The broad cytoplasmic assertion is biologically sound.

Reason: The broad cytoplasmic assertion is biologically sound. Independent target evidence supports soluble cytosolic and recycling-endosome membrane pools. These specify the cytoplasmic compartment without claiming exhaustive coverage of every original cell or all five products. Clathrin-coated-pit localization remains positively supported in its separate annotations and the motor core; it is not included in this replacement because a plasma-membrane pit is outside the current cytoplasm definition. The original PAINT, UniProt or rat-orthology source is preserved.

Proposed replacements: cytosol recycling endosome membrane

Summary: The broad cytoplasmic assertion is biologically sound.

Reason: The broad cytoplasmic assertion is biologically sound. Independent target evidence supports soluble cytosolic and recycling-endosome membrane pools. These specify the cytoplasmic compartment without claiming exhaustive coverage of every original cell or all five products. Clathrin-coated-pit localization remains positively supported in its separate annotations and the motor core; it is not included in this replacement because a plasma-membrane pit is outside the current cytoplasm definition. The original PAINT, UniProt or rat-orthology source is preserved.

Proposed replacements: cytosol recycling endosome membrane

Summary: The broad cytoplasmic assertion is biologically sound.

Reason: The broad cytoplasmic assertion is biologically sound. Independent target evidence supports soluble cytosolic and recycling-endosome membrane pools. These specify the cytoplasmic compartment without claiming exhaustive coverage of every original cell or all five products. Clathrin-coated-pit localization remains positively supported in its separate annotations and the motor core; it is not included in this replacement because a plasma-membrane pit is outside the current cytoplasm definition. The original PAINT, UniProt or rat-orthology source is preserved.

Proposed replacements: cytosol recycling endosome membrane

Summary: DNM2 associates with endocytic compartments.

Reason: DNM2 associates with endocytic compartments. PMID:32315611 more specifically demonstrates recruitment to recycling endosomes and release of nascent autophagic structures. Refine the gene-level location to recycling endosome membrane while preserving the original broader evidence; this does not assert that every endosomal DNM2 pool in the earlier experiment was the same compartment.

Proposed replacements: recycling endosome membrane

Summary: DNM2 associates with endocytic compartments.

Reason: DNM2 associates with endocytic compartments. PMID:32315611 more specifically demonstrates recruitment to recycling endosomes and release of nascent autophagic structures. Refine the gene-level location to recycling endosome membrane while preserving the original broader evidence; this does not assert that every endosomal DNM2 pool in the earlier experiment was the same compartment.

Proposed replacements: recycling endosome membrane

Summary: Centrosomal DNM2 is supported by the curated localization and the direct centrosome study PMID:15048127.

Reason: Centrosomal DNM2 is supported by the curated localization and the direct centrosome study PMID:15048127. Retain this specialized pool. The reduced labeling of selected disease variants is not absence of wild-type DNM2, and centrosome cohesion does not establish microtubule nucleation.

Summary: Centrosomal DNM2 is supported by the curated localization and the direct centrosome study PMID:15048127.

Reason: Centrosomal DNM2 is supported by the curated localization and the direct centrosome study PMID:15048127. Retain this specialized pool. The reduced labeling of selected disease variants is not absence of wild-type DNM2, and centrosome cohesion does not establish microtubule nucleation.

Summary: PMID:15048127 reports centriole-associated DNM2 by ultrastructural localization and implicates it in centrosome cohesion.

Reason: PMID:15048127 reports centriole-associated DNM2 by ultrastructural localization and implicates it in centrosome cohesion. Retain centriole localization as a context-specific pool; do not turn this into autonomous nucleation or a separate microtubule motor function.

Summary: PMID:15048127 reports centriole-associated DNM2 by ultrastructural localization and implicates it in centrosome cohesion.

Reason: PMID:15048127 reports centriole-associated DNM2 by ultrastructural localization and implicates it in centrosome cohesion. Retain centriole localization as a context-specific pool; do not turn this into autonomous nucleation or a separate microtubule motor function.

Summary: The actual HPA DNM2 record independently identifies cytosol as a main subcellular location, alongside Golgi apparatus.

Reason: The actual HPA DNM2 record independently identifies cytosol as a main subcellular location, alongside Golgi apparatus. Cytosolic DNM2 is a directly supported pool from which membrane-remodeling machinery is recruited; antibody-based localization does not distinguish every splice product.

Summary: PMID:18388313 uses cellular SNX9-DNM2 recruitment and tubulation assays; independent human cytosolic fractionation in PMID:15703209 and HPA support the same gene-level location.

Reason: PMID:18388313 uses cellular SNX9-DNM2 recruitment and tubulation assays; independent human cytosolic fractionation in PMID:15703209 and HPA support the same gene-level location. Retain cytosol, while not identifying every COS-7 construct as human.

Summary: Reactome:R-HSA-2130619 records DNM2 in the cytosolic trafficking machinery.

Reason: Reactome:R-HSA-2130619 records DNM2 in the cytosolic trafficking machinery. Exact event/entity paths are documented where recoverable; some endpoint requests were rate-limited and are not treated as biological absences. Independent human fractionation and HPA establish the cytosolic pool, so retain the location without claiming this proves a freely soluble state for every membrane-bound reaction intermediate.

Summary: Reactome:R-HSA-2130641 records DNM2 in the cytosolic trafficking machinery.

Reason: Reactome:R-HSA-2130641 records DNM2 in the cytosolic trafficking machinery. Exact event/entity paths are documented where recoverable; some endpoint requests were rate-limited and are not treated as biological absences. Independent human fractionation and HPA establish the cytosolic pool, so retain the location without claiming this proves a freely soluble state for every membrane-bound reaction intermediate.

Summary: Reactome:R-HSA-421831 records DNM2 in the cytosolic trafficking machinery.

Reason: Reactome:R-HSA-421831 records DNM2 in the cytosolic trafficking machinery. Exact event/entity paths are documented where recoverable; some endpoint requests were rate-limited and are not treated as biological absences. Independent human fractionation and HPA establish the cytosolic pool, so retain the location without claiming this proves a freely soluble state for every membrane-bound reaction intermediate.

Summary: Reactome:R-HSA-421835 records DNM2 in the cytosolic trafficking machinery.

Reason: Reactome:R-HSA-421835 records DNM2 in the cytosolic trafficking machinery. Exact event/entity paths are documented where recoverable; some endpoint requests were rate-limited and are not treated as biological absences. Independent human fractionation and HPA establish the cytosolic pool, so retain the location without claiming this proves a freely soluble state for every membrane-bound reaction intermediate.

Summary: Reactome:R-HSA-432706 records DNM2 in the cytosolic trafficking machinery.

Reason: Reactome:R-HSA-432706 records DNM2 in the cytosolic trafficking machinery. Exact event/entity paths are documented where recoverable; some endpoint requests were rate-limited and are not treated as biological absences. Independent human fractionation and HPA establish the cytosolic pool, so retain the location without claiming this proves a freely soluble state for every membrane-bound reaction intermediate.

Summary: Reactome:R-HSA-432707 records DNM2 in the cytosolic trafficking machinery.

Reason: Reactome:R-HSA-432707 records DNM2 in the cytosolic trafficking machinery. Exact event/entity paths are documented where recoverable; some endpoint requests were rate-limited and are not treated as biological absences. Independent human fractionation and HPA establish the cytosolic pool, so retain the location without claiming this proves a freely soluble state for every membrane-bound reaction intermediate.

Summary: Reactome:R-HSA-8868236 records DNM2 in the cytosolic trafficking machinery.

Reason: Reactome:R-HSA-8868236 records DNM2 in the cytosolic trafficking machinery. Exact event/entity paths are documented where recoverable; some endpoint requests were rate-limited and are not treated as biological absences. Independent human fractionation and HPA establish the cytosolic pool, so retain the location without claiming this proves a freely soluble state for every membrane-bound reaction intermediate.

Summary: Reactome:R-HSA-8868648 records DNM2 in the cytosolic trafficking machinery.

Reason: Reactome:R-HSA-8868648 records DNM2 in the cytosolic trafficking machinery. Exact event/entity paths are documented where recoverable; some endpoint requests were rate-limited and are not treated as biological absences. Independent human fractionation and HPA establish the cytosolic pool, so retain the location without claiming this proves a freely soluble state for every membrane-bound reaction intermediate.

Summary: Reactome:R-HSA-8868651 records DNM2 in the cytosolic trafficking machinery.

Reason: Reactome:R-HSA-8868651 records DNM2 in the cytosolic trafficking machinery. Exact event/entity paths are documented where recoverable; some endpoint requests were rate-limited and are not treated as biological absences. Independent human fractionation and HPA establish the cytosolic pool, so retain the location without claiming this proves a freely soluble state for every membrane-bound reaction intermediate.

Summary: Reactome:R-HSA-8868658 records DNM2 in the cytosolic trafficking machinery.

Reason: Reactome:R-HSA-8868658 records DNM2 in the cytosolic trafficking machinery. Exact event/entity paths are documented where recoverable; some endpoint requests were rate-limited and are not treated as biological absences. Independent human fractionation and HPA establish the cytosolic pool, so retain the location without claiming this proves a freely soluble state for every membrane-bound reaction intermediate.

Summary: Reactome:R-HSA-8868659 records DNM2 in the cytosolic trafficking machinery.

Reason: Reactome:R-HSA-8868659 records DNM2 in the cytosolic trafficking machinery. Exact event/entity paths are documented where recoverable; some endpoint requests were rate-limited and are not treated as biological absences. Independent human fractionation and HPA establish the cytosolic pool, so retain the location without claiming this proves a freely soluble state for every membrane-bound reaction intermediate.

Summary: Reactome:R-HSA-8868660 records DNM2 in the cytosolic trafficking machinery.

Reason: Reactome:R-HSA-8868660 records DNM2 in the cytosolic trafficking machinery. Exact event/entity paths are documented where recoverable; some endpoint requests were rate-limited and are not treated as biological absences. Independent human fractionation and HPA establish the cytosolic pool, so retain the location without claiming this proves a freely soluble state for every membrane-bound reaction intermediate.

Summary: Reactome:R-HSA-8868661 records DNM2 in the cytosolic trafficking machinery.

Reason: Reactome:R-HSA-8868661 records DNM2 in the cytosolic trafficking machinery. Exact event/entity paths are documented where recoverable; some endpoint requests were rate-limited and are not treated as biological absences. Independent human fractionation and HPA establish the cytosolic pool, so retain the location without claiming this proves a freely soluble state for every membrane-bound reaction intermediate.

Summary: Reactome:R-HSA-8869438 records DNM2 in the cytosolic trafficking machinery.

Reason: Reactome:R-HSA-8869438 records DNM2 in the cytosolic trafficking machinery. Exact event/entity paths are documented where recoverable; some endpoint requests were rate-limited and are not treated as biological absences. Independent human fractionation and HPA establish the cytosolic pool, so retain the location without claiming this proves a freely soluble state for every membrane-bound reaction intermediate.

Summary: Reactome:R-HSA-8871193 records DNM2 in the cytosolic trafficking machinery.

Reason: Reactome:R-HSA-8871193 records DNM2 in the cytosolic trafficking machinery. Exact event/entity paths are documented where recoverable; some endpoint requests were rate-limited and are not treated as biological absences. Independent human fractionation and HPA establish the cytosolic pool, so retain the location without claiming this proves a freely soluble state for every membrane-bound reaction intermediate.

Summary: Reactome:R-HSA-8871194 records DNM2 in the cytosolic trafficking machinery.

Reason: Reactome:R-HSA-8871194 records DNM2 in the cytosolic trafficking machinery. Exact event/entity paths are documented where recoverable; some endpoint requests were rate-limited and are not treated as biological absences. Independent human fractionation and HPA establish the cytosolic pool, so retain the location without claiming this proves a freely soluble state for every membrane-bound reaction intermediate.

Summary: Reactome:R-HSA-8951498 records DNM2 in the cytosolic trafficking machinery.

Reason: Reactome:R-HSA-8951498 records DNM2 in the cytosolic trafficking machinery. Exact event/entity paths are documented where recoverable; some endpoint requests were rate-limited and are not treated as biological absences. Independent human fractionation and HPA establish the cytosolic pool, so retain the location without claiming this proves a freely soluble state for every membrane-bound reaction intermediate.

Summary: The general cytoskeleton mapping can be specified to the microtubule-associated pool.

Reason: The source mapping is refined to independently supported microtubule localization. Focal-adhesion detection remains in its own positive contextual annotation; a cell–substrate junction is not established as a polymeric cytoskeletal structure merely because it attaches to the cytoskeleton. This source-specific replacement does not erase the adhesion pool, assign a second microtubule motor activity, or claim universal cellular distribution.

Proposed replacements: microtubule

Summary: Microtubule association is supported by the curated target experiments and the valid PAINT ancestral placement.

Reason: Microtubule association is supported by the curated target experiments and the valid PAINT ancestral placement. The PEX14-centered PMID:21525035 abstract does not expose its DNM2 assay, so it is not used to allege a paralog error. Retain a contextual microtubule-associated pool; no direct microtubule transport activity is inferred.

Summary: Microtubule association is supported by the curated target experiments and the valid PAINT ancestral placement.

Reason: Microtubule association is supported by the curated target experiments and the valid PAINT ancestral placement. The PEX14-centered PMID:21525035 abstract does not expose its DNM2 assay, so it is not used to allege a paralog error. Retain a contextual microtubule-associated pool; no direct microtubule transport activity is inferred.

Summary: Microtubule association is supported by the curated target experiments and the valid PAINT ancestral placement.

Reason: Microtubule association is supported by the curated target experiments and the valid PAINT ancestral placement. The PEX14-centered PMID:21525035 abstract does not expose its DNM2 assay, so it is not used to allege a paralog error. Retain a contextual microtubule-associated pool; no direct microtubule transport activity is inferred.

Summary: DNM2 acts at the cytoplasmic face of the plasma membrane during endocytic budding and scission.

Reason: DNM2 acts at the cytoplasmic face of the plasma membrane during endocytic budding and scission. The PAINT or Reactome placement is consistent with direct membrane-fission and endocytosis evidence. Retain the location without implying an integral transmembrane topology.

Summary: DNM2 acts at the cytoplasmic face of the plasma membrane during endocytic budding and scission.

Reason: DNM2 acts at the cytoplasmic face of the plasma membrane during endocytic budding and scission. The PAINT or Reactome placement is consistent with direct membrane-fission and endocytosis evidence. Retain the location without implying an integral transmembrane topology.

Summary: DNM2 acts at the cytoplasmic face of the plasma membrane during endocytic budding and scission.

Reason: DNM2 acts at the cytoplasmic face of the plasma membrane during endocytic budding and scission. The PAINT or Reactome placement is consistent with direct membrane-fission and endocytosis evidence. Retain the location without implying an integral transmembrane topology.

Summary: DNM2 acts at the cytoplasmic face of the plasma membrane during endocytic budding and scission.

Reason: DNM2 acts at the cytoplasmic face of the plasma membrane during endocytic budding and scission. The PAINT or Reactome placement is consistent with direct membrane-fission and endocytosis evidence. Retain the location without implying an integral transmembrane topology.

Summary: Clathrin-coated pits are a principal site of DNM2 recruitment and vesicle scission.

Reason: Clathrin-coated pits are a principal site of DNM2 recruitment and vesicle scission. The UniProt or rat-orthology mapping is concordant with SNX9-dependent recruitment and receptor-endocytosis evidence; retain this core location.

Summary: Clathrin-coated pits are a principal site of DNM2 recruitment and vesicle scission.

Reason: Clathrin-coated pits are a principal site of DNM2 recruitment and vesicle scission. The UniProt or rat-orthology mapping is concordant with SNX9-dependent recruitment and receptor-endocytosis evidence; retain this core location.

Summary: PMID:21423176 profiles adhesion fractions from human fibroblasts with replicate and false-discovery controls.

Reason: PMID:21423176 profiles adhesion fractions from human fibroblasts with replicate and false-discovery controls. Retain the curated DNM2 detection as a focal-adhesion context, supported independently by dynamin/cortactin adhesion biology. The target-resolved supplementary row was not independently recovered, so this is not a claim of direct imaging in that proteomic experiment.

Summary: PMID:10893263 shows that overexpressed rat Dyn2 ba in human-cell and mouse comparison systems can promote p53 accumulation, transcriptional responses and apoptosis, with GTPase-dependent effects.

Reason: PMID:10893263 shows that overexpressed rat Dyn2 ba in human-cell and mouse comparison systems can promote p53 accumulation, transcriptional responses and apoptosis, with GTPase-dependent effects. Preserve this experimental perturbation context as non-core; it does not establish DNM2 as a DNA-binding transcription factor or show that normal endogenous abundance universally drives the same outcome.

Summary: The Reactome post-Golgi pathway contains DNM2-dependent budding steps.

Reason: The Reactome post-Golgi pathway contains DNM2-dependent budding steps. PMID:18923138 independently reports cargo export and splice-dependent Golgi targeting in knockout/reconstitution experiments. Retain post-Golgi transport as an additional trafficking context rather than assume that every product or cargo uses an identical mechanism.

Summary: The source uses a viral-entry cell model and DNM2 WT/K44A perturbations; those findings do not alone specify all endocytic routes.

Reason: The source uses a viral-entry cell model and DNM2 WT/K44A perturbations; those findings do not alone specify all endocytic routes. Receptor-mediated endocytosis is a well-supported more specific DNM2 process, independently demonstrated by human-cell depletion and receptor-cargo uptake. This refinement does not imply that every source phenotype was measured with the same receptor.

Proposed replacements: receptor-mediated endocytosis

Summary: The ARBA electronic inference is consistent with the established dynamin trafficking machinery; incomplete reconstruction of a particular rule clause is not evidence that the biology is false.

Reason: The ARBA electronic inference is consistent with the established dynamin trafficking machinery; incomplete reconstruction of a particular rule clause is not evidence that the biology is false. Receptor-mediated endocytosis is a well-supported more specific DNM2 process, independently demonstrated by human-cell depletion and receptor-cargo uptake. This refinement does not imply that every source phenotype was measured with the same receptor.

Proposed replacements: receptor-mediated endocytosis

Summary: The cited source directly distinguishes receptor uptake from the tested Golgi pathway.

Reason: The cited source directly distinguishes receptor uptake from the tested Golgi pathway. Receptor-mediated endocytosis is a well-supported more specific DNM2 process, independently demonstrated by human-cell depletion and receptor-cargo uptake. This refinement does not imply that every source phenotype was measured with the same receptor.

Proposed replacements: receptor-mediated endocytosis

Summary: The Shank source discusses endocytosis in the specific context of postsynaptic membrane turnover.

Reason: The Shank source discusses endocytosis in the specific context of postsynaptic membrane turnover. Receptor-mediated endocytosis is a well-supported more specific DNM2 process, independently demonstrated by human-cell depletion and receptor-cargo uptake. This refinement does not imply that every source phenotype was measured with the same receptor.

Proposed replacements: receptor-mediated endocytosis

Summary: DNM2 contributes mechanical membrane scission to receptor-mediated endocytosis.

Reason: DNM2 contributes mechanical membrane scission to receptor-mediated endocytosis. Human disease-cell and depletion studies, together with purified human motor assays, support the gene-level process. Preserve the source-specific mutant, rodent muscle-cell, or rat-orthology context; necessity data alone are not the basis for this assignment because DNM2 performs the fission step.

Summary: DNM2 contributes mechanical membrane scission to receptor-mediated endocytosis.

Reason: DNM2 contributes mechanical membrane scission to receptor-mediated endocytosis. Human disease-cell and depletion studies, together with purified human motor assays, support the gene-level process. Preserve the source-specific mutant, rodent muscle-cell, or rat-orthology context; necessity data alone are not the basis for this assignment because DNM2 performs the fission step.

Summary: DNM2 contributes mechanical membrane scission to receptor-mediated endocytosis.

Reason: DNM2 contributes mechanical membrane scission to receptor-mediated endocytosis. Human disease-cell and depletion studies, together with purified human motor assays, support the gene-level process. Preserve the source-specific mutant, rodent muscle-cell, or rat-orthology context; necessity data alone are not the basis for this assignment because DNM2 performs the fission step.

Summary: DNM2 contributes mechanical membrane scission to receptor-mediated endocytosis.

Reason: DNM2 contributes mechanical membrane scission to receptor-mediated endocytosis. Human disease-cell and depletion studies, together with purified human motor assays, support the gene-level process. Preserve the source-specific mutant, rodent muscle-cell, or rat-orthology context; necessity data alone are not the basis for this assignment because DNM2 performs the fission step.

Summary: DNM2 releases nascent autophagosomes from recycling endosomes during macroautophagy.

Reason: The original study places DNM2 at LC3/RAB11A junctions and supports LC3-dependent scission and release with live imaging, depletion and recruitment-defective rescue. The HaloTag completion assay found unchanged open-phagophore numbers but accumulated completed autophagosomes and fewer autolysosomes; LC3 vesicles failed to detach. This supports macroautophagy, rather than assigning DNM2 the formation or closure of the double membrane. The paper explicitly separates this LC3 route from SNX18-dependent ATG9A traffic, which was not disrupted by these mutants. PI3P/Atg8 removal and directed autophagosome transport were not demonstrated, so maturation or localization terms are not substituted. Human endogenous evidence, rat HA constructs, current human recombinant-protein identity and unresolved gifted GFP-template species remain distinct.

Proposed replacements: macroautophagy

Summary: DNM2 recruitment supplies membrane carriers for autophagosome assembly.

Reason: Human-cell SNX18 WT versus DNM2-binding-deficient W38K experiments connect DNM2 recruitment to ATG9A exit from recycling endosomes, ATG16L1 recruitment and autophagic flux. DNM2 contributes mechanical carrier production supplying membranes for autophagosome assembly; it is not simply a cargo or a generic perturbation requirement. These are interaction-dependent trafficking/rescue assays, not a purified DNM2 fission assay. The later LC3-dependent release of completed autophagosomes in PMID:32315611 is a separate route and is not used to establish early formation here. The gifted dynamin-template species remains unresolved; no lipidation, engulfment or final closure activity is inferred.

Proposed replacements: autophagosome assembly

Summary: Rat DNM2 donor evidence links the protein to centrosome cohesion, consistent with PMID:15048127.

Reason: Rat DNM2 donor evidence links the protein to centrosome cohesion, consistent with PMID:15048127. Retain this specialized centrosome-cycle context; it does not show a direct microtubule-nucleation reaction or require a separate catalytic core.

Summary: PMID:10893263 shows that overexpressed rat Dyn2 ba in human-cell and mouse comparison systems can promote p53 accumulation, transcriptional responses and apoptosis, with GTPase-dependent effects.

Reason: PMID:10893263 shows that overexpressed rat Dyn2 ba in human-cell and mouse comparison systems can promote p53 accumulation, transcriptional responses and apoptosis, with GTPase-dependent effects. Preserve this experimental perturbation context as non-core; it does not establish DNM2 as a DNA-binding transcription factor or show that normal endogenous abundance universally drives the same outcome.

Summary: Microtubule binding is a retained ancillary dynamin property.

Reason: Microtubule binding is a retained ancillary dynamin property. The PAINT assertion traces to PTN000170013 with a literal Drosophila experimental donor; target microtubule association provides independent concordance. The source is not rejected because it has one donor, and target localization alone is not called a purified binding assay. This does not establish DNM2 as a microtubule translocation motor.

Summary: Microtubule binding is a retained ancillary dynamin property.

Reason: Microtubule binding is a retained ancillary dynamin property. The PAINT assertion traces to PTN000170013 with a literal Drosophila experimental donor; target microtubule association provides independent concordance. The source is not rejected because it has one donor, and target localization alone is not called a purified binding assay. This does not establish DNM2 as a microtubule translocation motor.

Summary: DNM2 has defined Golgi and recycling-endosome membrane pools within the endomembrane system.

Reason: DNM2 has defined Golgi and recycling-endosome membrane pools within the endomembrane system. Refine the general rule-derived location to these supported compartments; this is a target-level synthesis rather than a reconstruction of every condition in the ARBA rule.

Proposed replacements: Golgi membrane recycling endosome membrane

Summary: The Shank/ProSAP study provides postsynaptic-density fractionation and localization evidence in rat brain, consistent with the curated orthology and UniProt mappings.

Reason: The Shank/ProSAP study provides postsynaptic-density fractionation and localization evidence in rat brain, consistent with the curated orthology and UniProt mappings. Retain this neuronal context without recasting it as direct human tissue imaging or excluding other neuronal compartments.

Summary: The Shank/ProSAP study provides postsynaptic-density fractionation and localization evidence in rat brain, consistent with the curated orthology and UniProt mappings.

Reason: The Shank/ProSAP study provides postsynaptic-density fractionation and localization evidence in rat brain, consistent with the curated orthology and UniProt mappings. Retain this neuronal context without recasting it as direct human tissue imaging or excluding other neuronal compartments.

Summary: The broad membrane mapping can be refined to the established plasma, Golgi and recycling-endosome membrane contexts.

Reason: The broad membrane mapping can be refined to the established plasma, Golgi and recycling-endosome membrane contexts. DNM2 is recruited peripherally to membranes rather than being an integral membrane protein, and the replacements do not claim every membrane-associated pool has been enumerated.

Proposed replacements: plasma membrane Golgi membrane recycling endosome membrane

Summary: The literal PAINT IBD at PTN000902093 places synaptic-vesicle budding on an ancestor of DNM2, with Drosophila shibire experimental grounding.

Reason: The literal PAINT IBD at PTN000902093 places synaptic-vesicle budding on an ancestor of DNM2, with Drosophila shibire experimental grounding. A single donor does not invalidate this phylogenetic judgment. Retain a neuronal-context function without claiming that DNM2 is the predominant mammalian presynaptic dynamin or that the rat postsynaptic study alone proves vesicle budding.

Summary: Vesicle-mediated transport is sound but broad.

Reason: Vesicle-mediated transport is sound but broad. DNM2 directly contributes to vesicle scission during receptor-mediated endocytosis and in other trafficking settings. Refine this electronic process annotation to the already represented scission and receptor-mediated uptake processes; this adds specificity without adding a new source assertion.

Proposed replacements: vesicle scission receptor-mediated endocytosis

Summary: PMID:18388313 supports binding to the SNX9 SH3 domain, corroborated by controlled SNX9/PRD experiments in PMID:15703209.

Reason: PMID:18388313 supports binding to the SNX9 SH3 domain, corroborated by controlled SNX9/PRD experiments in PMID:15703209. This interaction class is a recruitment and regulatory mechanism of the motor. Preserve the historical construct-species uncertainty; it does not erase the well-supported gene-level activity.

Summary: The Reactome MHC-II pathway uses endocytic trafficking machinery in antigen processing.

Reason: The Reactome MHC-II pathway uses endocytic trafficking machinery in antigen processing. Retain DNM2 participation in this cell-type and cargo context, without assigning peptide binding, antigen recognition or a separate immune-specific catalytic activity to the motor.

Summary: Enzyme binding is compatible with independently demonstrated DNM2 interaction with the nucleotide-regenerating kinase NME2.

Reason: Enzyme binding is compatible with independently demonstrated DNM2 interaction with the nucleotide-regenerating kinase NME2. The original Shank-centered NAS reference does not by itself establish that enzymatic partner. Retain this broader ancillary binding class with explicit independent support rather than pretend the Shank scaffold is an enzyme.

Summary: DNM2 can remain associated with nascent clathrin-coated vesicles during the budding/scission cycle.

Reason: DNM2 can remain associated with nascent clathrin-coated vesicles during the budding/scission cycle. Retain the curated location, while distinguishing this transient vesicular pool from its principal recruitment at coated pits; no separate vesicle coat structural activity is inferred.

Summary: DNM2 can remain associated with nascent clathrin-coated vesicles during the budding/scission cycle.

Reason: DNM2 can remain associated with nascent clathrin-coated vesicles during the budding/scission cycle. Retain the curated location, while distinguishing this transient vesicular pool from its principal recruitment at coated pits; no separate vesicle coat structural activity is inferred.

Summary: The rat donor is directly localized to growth cones in PMID:21210813, with dynamin-specific antibody controls.

Reason: The rat donor is directly localized to growth cones in PMID:21210813, with dynamin-specific antibody controls. Retain this ortholog-supported neuronal pool, not a claim that every human DNM2 splice product is growth-cone enriched.

Summary: Midbody localization is supported by the curated source and PMID:21195118, which reports displacement of endogenous dynamin II from the midbody and cytokinesis failure after a phosphomimetic perturbation.

Reason: Midbody localization is supported by the curated source and PMID:21195118, which reports displacement of endogenous dynamin II from the midbody and cytokinesis failure after a phosphomimetic perturbation. Retain this cell-cycle context separately from endocytic recruitment.

Summary: Midbody localization is supported by the curated source and PMID:21195118, which reports displacement of endogenous dynamin II from the midbody and cytokinesis failure after a phosphomimetic perturbation.

Reason: Midbody localization is supported by the curated source and PMID:21195118, which reports displacement of endogenous dynamin II from the midbody and cytokinesis failure after a phosphomimetic perturbation. Retain this cell-cycle context separately from endocytic recruitment.

Summary: PMID:21210813 directly measures rat hippocampal growth-cone morphology and axon length after expression of WT and interaction-deficient dynamin/cortactin constructs.

Reason: PMID:21210813 directly measures rat hippocampal growth-cone morphology and axon length after expression of WT and interaction-deficient dynamin/cortactin constructs. Retain regulation of axon extension as an ortholog-supported neuronal context; it is not a universal human developmental program or proof of a fixed direction of regulation.

Summary: The Reactome endocytic reaction places DNM2 on endocytic-vesicle membrane machinery, consistent with its membrane scission role.

Reason: The Reactome endocytic reaction places DNM2 on endocytic-vesicle membrane machinery, consistent with its membrane scission role. Retain the compartment without inferring an integral membrane segment or luminal topology.

Summary: The UniProt location mapping records DNM2 at phagosomal membranes.

Reason: The UniProt location mapping records DNM2 at phagosomal membranes. Phagosome-maturation evidence in PMID:18425118 provides a compatible ortholog/mammalian context, but does not by itself identify every human reagent. Retain the specialized localization without a new phagocytosis core.

Summary: Receptor internalization is directly supported by DNM2-dependent uptake in human cells and by its physical membrane-scission role.

Reason: Receptor internalization is directly supported by DNM2-dependent uptake in human cells and by its physical membrane-scission role. The PAINT node PTN002611550 contains the target and legitimate target experimental grounding. Retain the process without inferring receptor binding or excluding other dynamin-dependent trafficking.

Summary: Receptor internalization is directly supported by DNM2-dependent uptake in human cells and by its physical membrane-scission role.

Reason: Receptor internalization is directly supported by DNM2-dependent uptake in human cells and by its physical membrane-scission role. The PAINT node PTN002611550 contains the target and legitimate target experimental grounding. Retain the process without inferring receptor binding or excluding other dynamin-dependent trafficking.

Summary: PMID:14985334 uses transferrin-receptor cargo uptake to establish a DNM2 requirement.

Reason: PMID:14985334 uses transferrin-receptor cargo uptake to establish a DNM2 requirement. Retain transferrin transport as a specific receptor-cargo context of endocytosis, without giving the motor a transferrin-binding or iron-transport activity.

Summary: Rat hippocampal neurons in PMID:21210813 show DNM2 along neuronal processes and at growth cones, with isoform-selective antibody controls.

Reason: Rat hippocampal neurons in PMID:21210813 show DNM2 along neuronal processes and at growth cones, with isoform-selective antibody controls. Retain the ortholog-supported neuronal projection location without assuming uniform enrichment across all neuronal compartments.

Summary: PMID:10893263 shows that overexpressed rat Dyn2 ba in human-cell and mouse comparison systems can promote p53 accumulation, transcriptional responses and apoptosis, with GTPase-dependent effects.

Reason: PMID:10893263 shows that overexpressed rat Dyn2 ba in human-cell and mouse comparison systems can promote p53 accumulation, transcriptional responses and apoptosis, with GTPase-dependent effects. Preserve this experimental perturbation context as non-core; it does not establish DNM2 as a DNA-binding transcription factor or show that normal endogenous abundance universally drives the same outcome.

Summary: The donor evidence in PMID:35620056 uses rat DNM2 constructs in human podocytes and controlled actin-recovery assays; rat recombinant protein is examined separately.

Reason: The donor evidence in PMID:35620056 uses rat DNM2 constructs in human podocytes and controlled actin-recovery assays; rat recombinant protein is examined separately. Retain stress-fiber assembly as a context of membrane-actin organization, without calling those constructs human or inferring all mutants are catalytically inactive.

Summary: The valid PAINT synaptic placement and independent Shank/ProSAP-associated postsynaptic evidence support a neuronal synaptic pool.

Reason: The valid PAINT synaptic placement and independent Shank/ProSAP-associated postsynaptic evidence support a neuronal synaptic pool. Retain the broad location as non-core rather than collapse it to an exclusively pre- or postsynaptic compartment.

Summary: The valid PAINT synaptic placement and independent Shank/ProSAP-associated postsynaptic evidence support a neuronal synaptic pool.

Reason: The valid PAINT synaptic placement and independent Shank/ProSAP-associated postsynaptic evidence support a neuronal synaptic pool. Retain the broad location as non-core rather than collapse it to an exclusively pre- or postsynaptic compartment.

Summary: PMID:11583995 supports a postsynaptic membrane-associated DNM2 pool through Shank/ProSAP binding and rat postsynaptic-density evidence.

Reason: PMID:11583995 supports a postsynaptic membrane-associated DNM2 pool through Shank/ProSAP binding and rat postsynaptic-density evidence. Retain the curated location with that organism and biochemical-fraction scope, not as a claim of direct human brain imaging.

Summary: PMID:10893263 shows that overexpressed rat Dyn2 ba in human-cell and mouse comparison systems can promote p53 accumulation, transcriptional responses and apoptosis, with GTPase-dependent effects.

Reason: PMID:10893263 shows that overexpressed rat Dyn2 ba in human-cell and mouse comparison systems can promote p53 accumulation, transcriptional responses and apoptosis, with GTPase-dependent effects. Preserve this experimental perturbation context as non-core; it does not establish DNM2 as a DNA-binding transcription factor or show that normal endogenous abundance universally drives the same outcome.

Summary: The original Shank paper chiefly establishes postsynaptic association, while the phylogenetic record independently supports a dynamin contribution to synaptic-vesicle recycling.

Reason: The original Shank paper chiefly establishes postsynaptic association, while the phylogenetic record independently supports a dynamin contribution to synaptic-vesicle recycling. Retain synaptic-vesicle transport as a non-core neuronal context without claiming that the cited postsynaptic fractionation directly measured presynaptic vesicle transport.

Summary: Rat hippocampal expression and domain-deletion experiments in PMID:21210813 directly change growth-cone shape and axon morphology.

Reason: Rat hippocampal expression and domain-deletion experiments in PMID:21210813 directly change growth-cone shape and axon morphology. Retain the ortholog-supported morphogenesis context; this does not establish a unique human developmental function or assign the effect to all splice products.

Summary: PMID:34744632 directly examines DNM2 assembly and variant effects using rat templates.

Reason: PMID:34744632 directly examines DNM2 assembly and variant effects using rat templates. Independent purified human DNM2 experiments in PMID:36445308 show membrane-associated polymer organization and fission. Retain polymerization as part of the coupled motor mechanism without inferring equivalent assembly behavior for all natural products.

Summary: DNM2 acts on recycling-endosome membranes during release of nascent autophagic structures in PMID:32315611.

Reason: DNM2 acts on recycling-endosome membranes during release of nascent autophagic structures in PMID:32315611. Refine the organelle-level location to its membrane rather than imply a luminal DNM2 pool; retain the original source evidence and construct limitations.

Proposed replacements: recycling endosome membrane

Summary: DNM2 acts on recycling-endosome membranes during release of nascent autophagic structures in PMID:32315611.

Reason: DNM2 acts on recycling-endosome membranes during release of nascent autophagic structures in PMID:32315611. Refine the organelle-level location to its membrane rather than imply a luminal DNM2 pool; retain the original source evidence and construct limitations.

Proposed replacements: recycling endosome membrane

Summary: The broad membrane-organization pathway includes DNM2-mediated budding and fission reactions.

Reason: The broad membrane-organization pathway includes DNM2-mediated budding and fission reactions. Vesicle scission is the directly performed mechanical step and is already represented by an experimental source. Refine to that step rather than infer every membrane-organizing event for DNM2.

Proposed replacements: vesicle scission

Summary: PMID:19605363 directly demonstrates rat DNM2/cortactin-dependent actin-bundle remodeling and separately tests human U2OS depletion with rat rescue.

Reason: PMID:19605363 directly demonstrates rat DNM2/cortactin-dependent actin-bundle remodeling and separately tests human U2OS depletion with rat rescue. The authors do not fully separate human-cell actin phenotypes from endocytic effects. Retain actin filament bundle organization as a supported motor context without claiming all biochemical reagents were human.

Summary: The rat DNM2 donor is experimentally grounded in controlled actin-bundle assays, including PMIDs:19605363 and 35620056.

Reason: The rat DNM2 donor is experimentally grounded in controlled actin-bundle assays, including PMIDs:19605363 and 35620056. Preserve this valid ortholog transfer and distinguish rat protein biochemistry from human host-cell phenotypes; it does not imply all natural human products have identical activity.

Summary: PMID:19056867 profiles extracellular vesicles isolated from human urine.

Reason: PMID:19056867 profiles extracellular vesicles isolated from human urine. Retain the curated DNM2 detection as a contextual extracellular-vesicle association; the target-specific peptide row was not independently recovered. Neither absence of a secretion signal nor its intracellular motor role establishes contamination, and detection does not prove an active extracellular DNM2 function.

Summary: PMID:23533145 profiles extracellular vesicles isolated from human urine.

Reason: PMID:23533145 profiles extracellular vesicles isolated from human urine. Retain the curated DNM2 detection as a contextual extracellular-vesicle association; the target-specific peptide row was not independently recovered. Neither absence of a secretion signal nor its intracellular motor role establishes contamination, and detection does not prove an active extracellular DNM2 function.

Summary: Rat growth-cone imaging in PMID:21210813 resolves DNM2 at basal point contacts marked by adhesion proteins, and human adhesion proteomics independently supports a focal-adhesion context.

Reason: Rat growth-cone imaging in PMID:21210813 resolves DNM2 at basal point contacts marked by adhesion proteins, and human adhesion proteomics independently supports a focal-adhesion context. Focal adhesion is a more informative location than generic anchoring junction; this target-level synthesis does not establish every original junction as a focal adhesion.

Proposed replacements: focal adhesion

Summary: Rat growth-cone imaging in PMID:21210813 resolves DNM2 at basal point contacts marked by adhesion proteins, and human adhesion proteomics independently supports a focal-adhesion context.

Reason: Rat growth-cone imaging in PMID:21210813 resolves DNM2 at basal point contacts marked by adhesion proteins, and human adhesion proteomics independently supports a focal-adhesion context. Focal adhesion is a more informative location than generic anchoring junction; this target-level synthesis does not establish every original junction as a focal adhesion.

Proposed replacements: focal adhesion

Summary: PMID:24135484 tests human DNM2 constructs in BIN1-dependent cellular tubulation and zebrafish models; mutant interference is not a purified demonstration of autonomous human tubule generation.

Reason: PMID:24135484 tests human DNM2 constructs in BIN1-dependent cellular tubulation and zebrafish models; mutant interference is not a purified demonstration of autonomous human tubule generation. Independent rat DNM2 liposome assays in PMID:35620056 support membrane tubulation. Retain the property as a membrane-remodeling context with these separate assay scopes. Independently, PMID:36445308 identifies human Dyn2 isoform 1 in Methods and reports purified-protein liposome tubulation and helical assembly in Results; this corroborates the gene-level capacity without changing the older source’s construct or assay scope.

Summary: The rat donor is directly supported by membrane-tubulation assays in PMID:35620056, alongside strong dependence on the PH-domain lipid interaction.

Reason: The rat donor is directly supported by membrane-tubulation assays in PMID:35620056, alongside strong dependence on the PH-domain lipid interaction. Retain the ortholog-supported physical property without identifying the human BIN1 coexpression phenotype as the same purified assay. Independently, PMID:36445308 identifies human Dyn2 isoform 1 in Methods and reports purified-protein liposome tubulation and helical assembly in Results; this corroborates the gene-level capacity without changing the older source’s construct or assay scope.

Summary: The annotation follows the synaptic-vesicle-budding process to a presynaptic location.

Reason: The annotation follows the synaptic-vesicle-budding process to a presynaptic location. The underlying PAINT node is on the DNM2 lineage and is not invalid merely because the experimentally characterized fly donor is singular. Retain this neuronal context without claiming predominant mammalian presynaptic expression or excluding postsynaptic DNM2.

Summary: PMID:32315611 connects DNM2 to physical scission at recycling endosomes supplying autophagic precursors.

Reason: PMID:32315611 connects DNM2 to physical scission at recycling endosomes supplying autophagic precursors. Purified human DNM2 fission assays in PMID:36445308 independently support the motor step. Retain scission as core, preserving the rat cellular HA-construct and historical recombinant-lot limits in the original source.

Summary: The recovered PMID:18388313 Results show that overexpressed DNM2 suppresses SNX9-induced COS-7 membrane tubules, whereas K44A and the SNX9 SH3 perturbation alter this response.

Reason: The recovered PMID:18388313 Results show that overexpressed DNM2 suppresses SNX9-induced COS-7 membrane tubules, whereas K44A and the SNX9 SH3 perturbation alter this response. Retain negative regulation of membrane tubulation in that defined coexpression context; it does not contradict the ability of dynamin polymers to shape membranes in another assay.