GDAP1: selected original evidence

This page records source and construct limits behind the annotation reasons. Original raw contexts, dataset row locators and the qualified source manifest are retained in the compact archive; current counts and exact excerpts are in source evidence. The source guide records access scope and the PANTHER sources.

Membrane dynamics

PMID:16172208(https://doi.org/10.1083/jcb.200507087), selected Results/Methods: mouse constructs and endogenous assays support outer-membrane topology and fission. A human host cell does not change the construct species. PMID:21753178(https://pubmed.ncbi.nlm.nih.gov/21753178/), Methods, fusion Results and Figure 3 caption: dominant human variants impair fusion; this does not by itself identify normal GDAP1 as performing membrane merger. Neither paper's figure pixels or supplements were inspected.

PMID:23628762(https://pubmed.ncbi.nlm.nih.gov/23628762/), selected main Results/Methods and Figure 3/4 captions: GDAP1 depletion elongates peroxisomes; re-expression rescues, with HD1 integrity and Drp1/Mff dependence. These results support participation in peroxisomal fission, beyond necessity alone. Mouse N1E115 and transient-cell experiments remain distinct; the wild-type rescue construct's species is unresolved in the inspected text. This cellular evidence is unaffected by the separate liposome translation-mixture limitation. No autonomous GDAP1 scission activity is required for participation.

Construct-dependent biochemical evidence

PMID:27841286(https://doi.org/10.1038/srep36930), original Results, Methods and Table 1: human Sf21-derived T288X conjugates glutathione to selected model substrates, while T318X does not under the tested conditions. Reticulocyte-translated full-length protein deforms mitochondrial/peroxisomal lipid-mixture liposomes, unlike pure phosphatidylcholine, with HD1scr, T288X and untreated controls. This is translation mixture, not purified full-length reagent, and deformation is not completed scission. Exact wild-type reagent species/sequence and catalytic coupling remain unresolved. These are engineered proteins, distinct from the two natural products.

PMID:32274853(https://doi.org/10.1096/fj.202000110R), selected original biochemical and cellular sections: mouse fragments lack detectable glutathione binding by thermal stabilization/calorimetry. Human-protein overexpression in HeLa changes morphology; this is distinct from a native human catalytic assay or an assertion of universal inactivity.

PMID:42520938(https://doi.org/10.1016/j.jbc.2026.113378), selected original Results and Experimental sections: human soluble protein binds thapsic acid by DSF/MST, with pocket-mutant effects. Pocket closure is modeled, and endogenous ligand identity remains open. Results describe residues 20–316 whereas Methods describe 21–315; the discrepancy is retained. No supplement or figure pixels were inspected for these three papers.

Interaction evidence and partner classes

HuRI, associated with PMID:32296183(https://pubmed.ncbi.nlm.nih.gov/32296183/), supplies nine pairs, 30 export rows and 29 matching current IntAct rows. Its GDAP1 target is Q8TB36-2, ORF2560, ENST00000434412.2. These literal identifiers do not prove complete clone identity or functional uniqueness; the GOA target stays Q8TB36. The Q96PD2-2 partner/47–789 construct limit is preserved.

PMID:32814053(https://doi.org/10.1016/j.celrep.2020.108050), supplement mmc3, supplies 32 GDAP1 pairs across NN1.0 and NN1.0ext; these are two network projections, not independent biological replicates. Current IntAct yields 96 matching rows. Gene-level table identity does not settle every product or clone. Independent partner-class records are cited by UniProtKB accession in each annotation. A refined binding class assigns neither the partner's activity nor a physiological consequence to GDAP1. Generic-term removals preserve the positive interactions.

Locally checkable partner-class excerpts

The following short source excerpts establish partner class; the interaction sources remain HuRI (two refined pairs) and Haenig (15 refined pairs). They do not establish native colocalization or a physiological consequence. UniProt excerpts come from curated FUNCTION, SIMILARITY or CATALYTIC ACTIVITY text, never DR GO lines. Source hashes and exact local offsets are recorded in source evidence. The retained official response SHA256 is 8cf7d5b6c1682abb64c51c4ced8b36cc0d53df77e32fa514ba7bbbcb88de4b21. UniProt pointers below are relative to each linked accession record; the ledger also retains the original query pointers and exact evidence arrays. Experimental attribution describes UniProt curation, not a new reading of every cited assay. Isoform and clone limits in the interaction table remain unchanged.

PMID:25869671(https://doi.org/10.1083/jcb.201407130), selected Results and cloning/cosedimentation Methods: human full-length TAGLN2 constructs associate with actin structures, and recombinant His-tagged protein cosediments with F-actin. Mouse endogenous localization is a separate observation. Neither establishes GDAP1 actin activity. Original XML SHA256: 446c2d28c8e7ea1734de802b5e46dec1a31c3354fa94699654bdde3db03c2935.

PMID:26949185(https://doi.org/10.1016/j.cell.2016.02.026), Results P28–29 and Methods P40–41: recombinant BOKΔC-8xHIS permeabilizes Ni-coupled large unilamellar vesicles, with lipid-only and total-release controls. Exact recombinant species/sequence is unresolved in the inspected main Methods; human HCT116 loss experiments are separate cellular evidence. No natural full-length human channel preparation or GDAP1 pore activity is inferred. Original HTML SHA256: 9d417a345ec885b2a9d882ce5c48ca8fdd8ef02af059a55e1b9b0a97b760d845. Neither paper's figure pixels or supplements were inspected.

CLPP's mature matrix location is separated from GDAP1's usual cytosol-facing domain; its assay interaction does not resolve native access. HOXC4's nuclear location similarly leaves native encounter unresolved. FOXR1 has curated cytoplasmic as well as nuclear localization; IQUB's axonemal association is not a demonstrated membrane-separated lumen. No relocalization mechanism is assumed for any pair.

Location and donor limits

MitoCoP, PMID:34800366, supplementary Table S2 A row404/B row366, identifies the GDAP1 protein group; assay classifications support mitochondrial occurrence and integral association without unique isoform resolution. HPA metadata supports mitochondria plus cytosol; image pixels were not independently read.

Reactome 9603775, 9603784 and 9603804 were traced through every component/member edge to human Q8TB36 residues 1–358: cytosolic entity9603796 and membrane entity9603788. The genuine cached 9603798 model summary was also read during native reconciliation; its model-level support is distinct from a new primary experiment.

PMID:21630459(https://pubmed.ncbi.nlm.nih.gov/21630459/) is an authentic sperm-nucleus proteomics source, but its target-level evidence remains uninspected. The sperm extension is retained. PMID:25449168(https://pubmed.ncbi.nlm.nih.gov/25449168/) is a genuine rat INS-1 abundance-response source; human regulation and mechanistic participation are not established by that observation.

Scope of a possible membrane-bending annotation

GO:0180020 is molecular-function membrane bending activity; GO:0097753 is a biological process. The translation-mixture and wild-type reagent limits concern the autonomous membrane-bending assignment from PMID:27841286; they do not weaken the separate cellular peroxisomal-fission evidence. Human OPA1/CHMP2A/CHMP3 show that the MF is used for physical deformation. No GDAP1 GO-CAM entry was found in the inspected index.

Peroxisomal role and annotation provenance

Peroxisomal fission is supported biologically. PEX11B carries experimental and ancestral GO:0016559 annotations, so there is no inferred GO convention excluding a membrane-remodeling participant. The deferred decision concerns provenance for a new human annotation, not weak or negative biology.

Mitochondrial fission already has a human IDA curator assertion and an inspected PAINT IBD, retained with independent perturbation corroboration. PMID:15772096's abstract does not itself expose the fission assay; it is not presented as direct human evidence independently read here. Retaining that existing assertion is different from creating an experimental assertion. Assigning a new human IMP from the unresolved rescue construct would overstate its inspected provenance. A conserved-role inference would require an explicit inference/source judgment rather than silently relabeling the assay. No NEW is added in this bounded amendment; the positive peroxisomal role remains explicit in the biological description and source assessment.