Ataxin-2 is a predominantly cytoplasmic RNA-binding protein that associates with messenger ribonucleoproteins and regulates mRNA stability and translation. It contacts U-rich sequences in mRNA 3' untranslated regions and recruits PABPC1 and the cytoplasmic poly(A) polymerase TENT2 to selected transcripts, supporting poly(A)-tail extension and translation. Its RNA- and protein-interaction regions also influence stress-granule composition and assembly in a manner that depends on cell type and stress conditions. Polyglutamine expansion in ATXN2 causes spinocerebellar ataxia type 2.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0002091 negative regulation of receptor internalization | IMP PMID:18602463 Ataxin-2 associates with the endocytosis complex and affects... | KEEP AS NON CORE | Summary: ATXN2 modulates receptor trafficking in the tested endocytic system. Reason: The complete PMID18602463 abstract supports endocytic receptor cycling; the original publisher introductory passage explicitly reports reduced ligand-stimulated EGFR downregulation in its internalization analysis. Retain the curator's direction-specific IMP assertion as a secondary role. Detailed EGFR assay Methods and species of every construct remain uninspected; this is not a general claim about all receptors. |
| GO:0003723 RNA binding | HDA PMID:22658674 Insights into RNA biology from an atlas of mammalian mRNA-bi... | ACCEPT | Summary: The human HeLa mRNA-interactome screen supports the core RNA-binding property. Reason: PMID22658674 uses UV crosslinking and interactome capture. The exact ATXN2 supplementary entry was not independently recovered here, but direct human ATXN2 RNA contact is separately supported by PMID24954906. Accept the broad HDA property with curator deference; do not rewrite the original assay as a measured 3β²-UTR preference. The broad HDA measurement is retained at its original precision, unlike the separate IEA/NAS refinements based on direct target-RNA evidence. |
| GO:0003723 RNA binding | HDA PMID:22681889 The mRNA-bound proteome and its global occupancy profile on ... | ACCEPT | Summary: The human-cell mRNA-bound proteome supports RNA association. Reason: PMID22681889 reports photoreactive nucleotide-enhanced UV crosslinking and oligo(dT) capture in a human embryonic kidney cell line. Its ATXN2-specific supplementary entry is not independently inspected; the known RNA-binding property has independent direct support from PMID24954906. Keep the source's broad HDA assertion without attributing the later target-specific assay to this screen. The broad HDA measurement is retained at its original precision, unlike the separate IEA/NAS refinements based on direct target-RNA evidence. |
| GO:0003723 RNA binding | IEA GO_REF:0000002 | MODIFY | Summary: Independent direct target evidence allows a more informative RNA-binding term. Reason: The InterPro mapping identifies an RNA-binding family but does not itself establish a particular transcript segment. PMID24954906 independently reports ATXN2 contact with U-rich 3β²-UTR elements. Refine to mRNA 3β²-UTR binding using that explicit corroboration; do not infer the activity of each isolated LSmAD domain or every alternative product. Proposed replacements: mRNA 3'-UTR binding |
| GO:0003723 RNA binding | NAS PMID:10814712 A novel protein with RNA-binding motifs interacts with ataxi... | MODIFY | Summary: Later direct RNA-contact evidence resolves the broad early NAS claim. Reason: PMID10814712 primarily establishes association with A2BP1/RBFOX1, whose RNP motif must not be assigned to ATXN2. The essence of ATXN2 RNA binding is independently supported by PMID24954906, allowing refinement to mRNA 3β²-UTR binding. Retain the NAS source tuple and distinguish this corroboration from an experiment performed in the 2000 paper. Proposed replacements: mRNA 3'-UTR binding |
| GO:0003729 mRNA binding | IBA GO_REF:0000033 | ACCEPT | Summary: mRNA binding is a central ATXN2 activity. Reason: The PTN000304339 IBA expresses ancestral inheritance, not a vote based on the two displayed extant donors. Direct ATXN2 crosslinking in PMID24954906 agrees with the assertion. No phylogenetic-placement defect or target loss is alleged; the full family tree/MSA was not reconstructed, and the ancestral mRNA term need not be narrowed to the later human target preference. |
| GO:0005154 epidermal growth factor receptor binding | IPI PMID:18602463 Ataxin-2 associates with the endocytosis complex and affects... | UNDECIDED | Summary: The precise EGFR-binding assay remains unresolved. Reason: The PMID18602463 abstract distinguishes endophilin/CIN85/Src interactions from a functional EGFR-trafficking endpoint. The accessed publisher passage confirms receptor downregulation but does not show the exact ATXN2βEGFR binding experiment. Keep the curated P00533 source intact and use UNDECIDED rather than treating receptor trafficking as proof of binding or declaring misattribution. |
| GO:0005515 protein binding | IPI PMID:10814712 A novel protein with RNA-binding motifs interacts with ataxi... | KEEP AS NON CORE | Summary: A2BP1/RBFOX1 is a verified ATXN2 interaction partner. Reason: PMID10814712 directly describes the partner interaction and trans-Golgi colocalization. The generic interaction is supported but is not the mechanistic RNA-binding activity of ATXN2; no adaptor or RNA-recognition-motif activity is inferred from the partner. Supporting Evidence: PMID:10814712 A2BP1 (ataxin-2 binding protein 1) which binds to the C-terminus of ataxin-2. |
| GO:0005515 protein binding | IPI PMID:15663938 An integrative approach to gain insights into the cellular f... | KEEP AS NON CORE | Summary: PABPC1 associates with ATXN2 in the original interaction study. Reason: PMID15663938 reports yeast two-hybrid/coimmunoprecipitation and mammalian colocalization. Retain the supported interaction as non-core generic binding; translation-regulatory activity requires separate functional endpoints and is not established by association alone. |
| GO:0005515 protein binding | IPI PMID:16115810 Ataxin-2 and huntingtin interact with endophilin-A complexes... | MODIFY | Summary: The endophilin-A1 interaction has an independently mapped SH3 interface. Reason: PMID16115810 establishes ATXN2 association with endophilin-A1; PMID18602463 independently maps ATXN2 proline-rich regions to the endophilin SH3 domain. This supports SH3 domain binding, without inferring catalytic activity or a universal endocytic-scaffold role. The later domain mapping is corroboration, not an assay attributed to the original 2005 paper. Proposed replacements: SH3 domain binding |
| GO:0005515 protein binding | IPI PMID:16115810 Ataxin-2 and huntingtin interact with endophilin-A complexes... | MODIFY | Summary: The endophilin-A3 interaction has an independently mapped SH3 interface. Reason: PMID16115810 establishes ATXN2 association with endophilin-A3; PMID18602463 independently maps ATXN2 proline-rich regions to the endophilin SH3 domain. This supports SH3 domain binding, without inferring catalytic activity or a universal endocytic-scaffold role. The later domain mapping is corroboration, not an assay attributed to the original 2005 paper. Proposed replacements: SH3 domain binding |
| GO:0005515 protein binding | IPI PMID:16713569 A protein-protein interaction network for human inherited at... | UNDECIDED | Summary: The exact ATXN1/P54253 pair in the ataxia interaction network remains uninspected. Reason: PMID16713569 reports a large human yeast-two-hybrid network with validation of a subset, but the exact ATXN1/P54253 assignment and validation route were not independently recovered. Preserve this IPI source as unresolved. Independent interaction or domain mapping in a different paper is not an inspection of the network's target-level assignment and is not attributed to this source. |
| GO:0005515 protein binding | IPI PMID:16713569 A protein-protein interaction network for human inherited at... | UNDECIDED | Summary: The exact endophilin-A1/Q99962 pair in the ataxia interaction network remains uninspected. Reason: PMID16713569 reports a large human yeast-two-hybrid network with validation of a subset, but the exact endophilin-A1/Q99962 assignment and validation route were not independently recovered. Preserve this IPI source as unresolved. Independent interaction or domain mapping in a different paper is not an inspection of the network's target-level assignment and is not attributed to this source. |
| GO:0005515 protein binding | IPI PMID:16713569 A protein-protein interaction network for human inherited at... | UNDECIDED | Summary: The exact endophilin-A3/Q99963 pair in the ataxia interaction network remains uninspected. Reason: PMID16713569 reports a large human yeast-two-hybrid network with validation of a subset, but the exact endophilin-A3/Q99963 assignment and validation route were not independently recovered. Preserve this IPI source as unresolved. Independent interaction or domain mapping in a different paper is not an inspection of the network's target-level assignment and is not attributed to this source. |
| GO:0005515 protein binding | IPI PMID:17097639 Parkin is an E3 ubiquitin-ligase for normal and mutant ataxi... | KEEP AS NON CORE | Summary: Parkin binds and ubiquitinates ATXN2 as its substrate. Reason: PMID17097639 directly supports the interaction for normal and expanded constructs. Parkin supplies ubiquitin-ligase catalysis; this evidence does not make ATXN2 an E3 enzyme or establish a core ubiquitination role. Human-cell and mutant/brain endpoints remain distinct. |
| GO:0005515 protein binding | IPI PMID:17392519 Ataxin-2 interacts with the DEAD/H-box RNA helicase DDX6 and... | KEEP AS NON CORE | Summary: PABPC1 association is supported, while the abundance assay is a separate endpoint. Reason: PMID17392519 explicitly treats PABP as an ATXN2 partner and measures its abundance after ATXN2 perturbation; PMID15663938 and the PAM2βMLLE structure in PMID20181956 independently substantiate the interaction. Keep generic binding non-core and do not call changes in abundance intrinsic translational or degradation catalysis. |
| GO:0005515 protein binding | IPI PMID:17392519 Ataxin-2 interacts with the DEAD/H-box RNA helicase DDX6 and... | KEEP AS NON CORE | Summary: DDX6 association is directly supported in human-cell experiments. Reason: PMID17392519 Results maps the yeast-two-hybrid interaction to ATXN2 residues254β475 and detects reciprocal endogenous association in nuclease-treated HEK293T/SH-SY5Y lysates. This supports a real interaction without assigning DDX6 helicase catalysis to ATXN2. Supporting Evidence: PMID:17392519 an association between ATXN2 and DDX6 occurs in mammalian cells |
| GO:0005515 protein binding | IPI PMID:18602463 Ataxin-2 associates with the endocytosis complex and affects... | MODIFY | Summary: The endophilin-A1 interaction is resolved to its SH3 domain. Reason: The complete PMID18602463 abstract describes human-brain-library screening and maps ATXN2 proline-rich regions to endophilin-A1/A3 SH3 domains. GO0017124 explicitly describes binding to an SH3 domain and is a protein-domain-specific binding child. This is a justified refinement of the interaction; endogenous mouse-brain confirmation and rat-neuron localization remain separate from human construct inference. Proposed replacements: SH3 domain binding Supporting Evidence: PMID:18602463 which interacted with the SH3 domain of endophilin A1/A3. |
| GO:0005515 protein binding | IPI PMID:18602463 Ataxin-2 associates with the endocytosis complex and affects... | MODIFY | Summary: The endophilin-A3 interaction is resolved to its SH3 domain. Reason: The complete PMID18602463 abstract describes human-brain-library screening and maps ATXN2 proline-rich regions to endophilin-A1/A3 SH3 domains. GO0017124 explicitly describes binding to an SH3 domain and is a protein-domain-specific binding child. This is a justified refinement of the interaction; endogenous mouse-brain confirmation and rat-neuron localization remain separate from human construct inference. Proposed replacements: SH3 domain binding |
| GO:0005515 protein binding | IPI PMID:20181956 Structural basis of binding of P-body-associated proteins GW... | KEEP AS NON CORE | Summary: PABPC1 binds an ATXN2 PAM2 peptide through its MLLE domain. Reason: PMID20181956 reports structures and affinity/mutagenesis experiments with the PABPC1 domain and ATXN2-derived peptide. Preserve this specific interface evidence as non-core generic binding; it is not a test of every full-length natural ATXN2 isoform or of polymerase catalysis. |
| GO:0005515 protein binding | IPI PMID:20740007 Ataxin-2 intermediate-length polyglutamine expansions are as... | KEEP AS NON CORE | Summary: TDP-43 and ATXN2 associate in an RNA-dependent complex. Reason: PMID20740007 explicitly states the dependence on RNA. Retain the experimentally supported complex association with this limitation; do not call it an isolated binary interface or turn ALS-modifier effects into a new normal-function process. Supporting Evidence: PMID:20740007 ATXN2 and TDP-43 associate in a complex that depends on RNA. |
| GO:0005515 protein binding | IPI PMID:23209657 Ataxin-2-like is a regulator of stress granules and processi... | KEEP AS NON CORE | Summary: The ATXN2βG3BP interaction is explicitly tested despite the ATXN2L-focused title. Reason: PMID23209657 Results/Figure4B describes reciprocal endogenous ATXN2/G3BP immunoprecipitation in HEK293T and HeLa experiments. The annotation is not a paralog error. ATXN2L overexpression/knockdown phenotypes are distinct experiments and are not transferred wholesale to ATXN2. Supporting Evidence: PMID:23209657 endogenous G3BP was precipitated with an antibody directed against ATXN2 |
| GO:0005515 protein binding | IPI PMID:24981860 Human-chromatin-related protein interactions identify a deme... | UNDECIDED | Summary: The exact ATXN2βDDX6 pair in the chromatin-related interaction map needs its source table. Reason: PMID24981860 describes a broad human affinity-purification map; its title and abstract do not identify the queried pair. Independent DDX6 evidence does not certify the precise experiment in this dataset. Retain the source and defer rather than alleging a wrong-gene citation. |
| GO:0005515 protein binding | IPI PMID:26184334 Comprehensive Protein Interactome Analysis of a Key RNA Heli... | UNDECIDED | Summary: The PABPC1 pair assignment in the DDX6-centric study remains source-specific uncertainty. Reason: PMID26184334 Table1 includes ATXN2 and PABPC1 among DDX6-associated proteins, and the text cites a known ATXN2/ATXN2LβPABPC1 complex. The inspected DDX6-bait assay is not by itself a binary ATXN2βPABPC1 measurement. The direct interaction is established elsewhere, but the original pair-table route for this IPI row remains unresolved. |
| GO:0005515 protein binding | IPI PMID:26184334 Comprehensive Protein Interactome Analysis of a Key RNA Heli... | KEEP AS NON CORE | Summary: ATXN2 is explicitly recovered in the DDX6 interactome. Reason: PMID26184334 Results2.1/Table1 identifies ATXN2 among non-ribosomal, RNA-independent DDX6-associated proteins from nuclease-treated human HEK293 preparations. Retain the interaction as non-core and do not overstate every pulldown as a purified binary binding measurement. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | UNDECIDED | Summary: The ATXN2βDDX6 edge from BioPlex affinity-purification networks needs exact record inspection. Reason: The complete normal abstract for PMID33961781 was read, but its exact ATXN2/DDX6 target table and evidence route were not retrieved in this bounded audit. Proximity or complex association should not be promoted to binary binding. Preserve the curated IPI tuple and defer the source-specific decision; absence from the accessible narrative is not evidence of a false interaction. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | UNDECIDED | Summary: The ATXN2βDDX6 edge from OpenCell endogenous-tagging proteomics needs exact record inspection. Reason: The complete normal abstract for PMID35271311 was read, but its exact ATXN2/DDX6 target table and evidence route were not retrieved in this bounded audit. Proximity or complex association should not be promoted to binary binding. Preserve the curated IPI tuple and defer the source-specific decision; absence from the accessible narrative is not evidence of a false interaction. |
| GO:0005515 protein binding | IPI PMID:39251607 Systematic identification of post-transcriptional regulatory... | UNDECIDED | Summary: The ATXN2βDDX6 edge from proximity-labeling and multimodal regulatory modules needs exact record inspection. Reason: The complete normal abstract for PMID39251607 was read, but its exact ATXN2/DDX6 target table and evidence route were not retrieved in this bounded audit. Proximity or complex association should not be promoted to binary binding. Preserve the curated IPI tuple and defer the source-specific decision; absence from the accessible narrative is not evidence of a false interaction. |
| GO:0005737 cytoplasm | IDA PMID:10814712 A novel protein with RNA-binding motifs interacts with ataxi... | ACCEPT | Summary: ATXN2 has a cytoplasmic RNA-regulatory setting. Reason: PMID10814712 provides the original localization context, including trans-Golgi-associated staining; independent PMID17392519 documents diffuse cytoplasmic endogenous ATXN2 and stress-dependent redistribution. Cytoplasm is a valid core location across conditions, not an assertion of exclusive localization. |
| GO:0005737 cytoplasm | IDA PMID:10973246 Nuclear localization or inclusion body formation of ataxin-2... | ACCEPT | Summary: Cytoplasmic ATXN2 is supported in the human and model material examined. Reason: PMID10973246 explicitly distinguishes cytoplasmic ATXN2 from a required nuclear-inclusion mechanism. Retain the source localization while separating normal protein from expanded-mutant pathogenesis and transgenic mouse experiments. |
| GO:0005737 cytoplasm | IDA PMID:17392519 Ataxin-2 interacts with the DEAD/H-box RNA helicase DDX6 and... | ACCEPT | Summary: Endogenous ATXN2 is diffuse in the cytoplasm before stress. Reason: PMID17392519 Results explicitly reports cytoplasmic distribution in several mammalian cell lines and redistribution into stress granules after arsenite or heat. Retain the broad location because narrowing all protein to granules would erase the unstressed distribution. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: The UniProt cytoplasmic-location mapping matches the principal RNA-regulatory setting. Reason: This IEA vocabulary mapping agrees with direct endogenous localization in PMID17392519. A single narrower compartment would not cover the unstressed diffuse and stress-dependent granule populations, so no artificial specificity replacement is proposed. |
| GO:0005794 Golgi apparatus | IDA PMID:12812977 Expansion of the polyQ repeat in ataxin-2 alters its Golgi l... | KEEP AS NON CORE | Summary: Golgi association is a documented secondary localization. Reason: PMID12812977 directly compares ATXN2 Golgi localization and altered mutant localization in cell models. Retain the location but separate normal localization from expanded-polyglutamine Golgi disruption and cell death. |
| GO:0005794 Golgi apparatus | IDA PMID:17097639 Parkin is an E3 ubiquitin-ligase for normal and mutant ataxi... | KEEP AS NON CORE | Summary: The Parkin study is consistent with a Golgi-associated ATXN2 pool. Reason: PMID17097639 investigates Golgi morphology and ATXN2 localization in normal/expanded construct settings. The normal cache is abstract-only; independent PMID12812977 directly supports Golgi localization, so retain this secondary location with curator deference without claiming a complete figure or compartment-specific assay reread. |
| GO:0005802 trans-Golgi network | IDA PMID:10814712 A novel protein with RNA-binding motifs interacts with ataxi... | KEEP AS NON CORE | Summary: Trans-Golgi-associated ATXN2 is supported by the original A2BP1 study. Reason: PMID10814712 reports colocalization of A2BP1 and ATXN2 in the trans-Golgi network. This is a secondary localization; the later core RNA/granule model does not justify denying this experimentally reported compartment. |
| GO:0006417 regulation of translation | NAS PMID:16835262 Ataxin-2 and its Drosophila homolog, ATX2, physically assemb... | ACCEPT | Summary: Translation regulation is a central role supported beyond polysome association. Reason: PMID16835262 reports human ATXN2 and fly ATX2 polysome association, with a NAS interpretation of regulation. Later human reporter and polysome experiments in PMID32989052 independently establish translation activation. Keep the original NAS source distinct from the later direct functional endpoints; ATXN2 is not the catalytic poly(A) polymerase. |
| GO:0010494 cytoplasmic stress granule | IBA GO_REF:0000033 | ACCEPT | Summary: Stress-granule localization is both phylogenetically inferred and directly observed on ATXN2. Reason: The PTN000304339 IBA includes Q99700 among experimental descendant sources; that is expected PAINT grounding, not circularity. Human ATXN2 localization in PMID17392519 supports the inherited claim. The full tree/MSA was not independently reconstructed, and no loss or misplaced-node allegation is made. |
| GO:0010494 cytoplasmic stress granule | IDA PMID:17392519 Ataxin-2 interacts with the DEAD/H-box RNA helicase DDX6 and... | ACCEPT | Summary: Human-cell ATXN2 redistributes to cytoplasmic stress granules. Reason: PMID17392519 Results shows endogenous ATXN2 colocalizing with TIA-1/DDX6 after heat or arsenite, with a DCP1 comparison distinguishing P-bodies. This localization does not imply that ATXN2 is universally indispensable for granule formation. |
| GO:0016020 membrane | HDA PMID:19946888 Defining the membrane proteome of NK cells. | KEEP AS NON CORE | Summary: Keep the broad membrane-proteome observation with its original precision. Reason: PMID19946888 reports isolated YTS-cell membranes and includes transiently associated proteins; its exact ATXN2 target table remains uninspected. Independent PMID18602463 reports ER/plasma-membrane association in transfected cell lines, with mouse-brain fractionation and a conserved pattern in rat neurons. This positively corroborates a non-core membrane association without substituting another paper's compartment or species for the original broad HDA assertion. No integral-membrane topology is inferred. |
| GO:0016070 RNA metabolic process | NAS PMID:15663938 An integrative approach to gain insights into the cellular f... | MODIFY | Summary: Translation regulation is more informative than the broad RNA-metabolism NAS term. Reason: PMID15663938 supports a conserved PABP-associated role, while PMID16835262 and later human functional PMID32989052 support translation regulation. Refine the broad process to GO0006417 using explicit independent corroboration; do not assign every yeast Pbp1 phenotype or direct RNA-processing catalysis to human ATXN2. Proposed replacements: regulation of translation |
| GO:0033962 P-body assembly | IMP PMID:17392519 Ataxin-2 interacts with the DEAD/H-box RNA helicase DDX6 and... | MODIFY | Summary: Elevated ATXN2 reduces visible P-bodies rather than demonstrating a structural assembly role. Reason: The actual PMID17392519 Results compares full-length normal/expanded constructs and the DDX6-binding region; overexpression reduces P-body structures, whereas lowered ATXN2 has no obvious P-body effect. GO0010607 captures the direction-specific regulatory phenotype. This is a replacement of an existing IMP assertion, not a NEW process, and it does not establish universal physiological P-body suppression. Proposed replacements: negative regulation of cytoplasmic mRNA processing body assembly Supporting Evidence: PMID:17392519 the number of P-bodies present was greatly reduced |
| GO:0034063 cytoplasmic stress granule assembly | IBA GO_REF:0000033 | ACCEPT | Summary: The inherited granule-assembly contribution agrees with direct target perturbation. Reason: The PTN000304339 IBA is not weakened by the displayed target Q99700 or by the short donor list. PMID17392519 gives an actual ATXN2-dependent change in granule number/size. Retain the contextual contribution without claiming complete loss of granules or a universally essential scaffold. Later human knockout and partial-depletion/rescue studies preserve granule formation while changing its properties, supporting a context-dependent contribution rather than universal necessity. |
| GO:0034063 cytoplasmic stress granule assembly | IMP PMID:17392519 Ataxin-2 interacts with the DEAD/H-box RNA helicase DDX6 and... | ACCEPT | Summary: ATXN2 depletion affects stress-granule assembly in the tested human cells. Reason: PMID17392519 reports reduced number/size in HEK293T RNAi experiments, with residual ATXN2/TIA-1-positive granules. This supports involvement in assembly under the tested conditions; later context-dependent findings need not negate the existing IMP assertion, and no universal necessity claim is made. Later human knockout and partial-depletion/rescue studies preserve granule formation while changing its properties, supporting a context-dependent contribution rather than universal necessity. |
| GO:0048471 perinuclear region of cytoplasm | IDA PMID:17097639 Parkin is an E3 ubiquitin-ligase for normal and mutant ataxi... | KEEP AS NON CORE | Summary: A perinuclear ATXN2 pool is a secondary localization rather than a separate core activity. Reason: Retain the PMID17097639 IDA compartment with curator deference, consistent with the independently documented Golgi-associated pool. The exact perinuclear figure was not independently inspected, so do not claim that the complete source Methods or images were verified. |
| GO:0050658 RNA transport | NAS PMID:10814712 A novel protein with RNA-binding motifs interacts with ataxi... | MARK AS OVER ANNOTATED | Summary: The original paper proposes neuronal RNA transport as a hypothesis rather than measuring RNA-cargo movement. Reason: The separately accessed author-deposited original PMID10814712 was read through Results, Discussion and Methods. Its proposed neuronal RNA-transport role is explicitly conditional; the experiments establish A2BP1 interaction, expression, fractionation and protein localization, without a transported RNA cargo or movement endpoint. RNA binding and translation regulation do not establish RNA transport. The NAS assertion therefore exceeds this source's evidence, without proving that ATXN2 cannot participate in transport. The normal cache remains abstract-only; the broader manual reading is recorded separately. |
| GO:1990904 ribonucleoprotein complex | IDA PMID:16835262 Ataxin-2 and its Drosophila homolog, ATX2, physically assemb... | ACCEPT | Summary: ATXN2 associates with translating ribonucleoprotein assemblies. Reason: PMID16835262 explicitly reports association with polyribosomes, distinguishing human ATXN2 from Drosophila ATX2 experiments. This supports the ribonucleoprotein-complex annotation without making ATXN2 a constitutive ribosomal structural subunit or transferring each fly deletion result to human isoforms. |
| GO:0008494 translation activator activity | IDA PMID:32989052 Direct evidence that Ataxin-2 is a translational activator m... | NEW | Summary: Human ATXN2 increases translation efficiency of associated reporter mRNAs. Reason: PMID32989052 tests reconstructed human full-length ATXN2 in HEK293T cells using mRNA-normalized reporter output and a selective shift of target RNA to heavier polysomes, with GAPDH unchanged. Recruitment of PABPC1 and TENT2/PAPD4 supports regulatory activation; TENT2 supplies polymerase catalysis. This molecular activity is distinct from the existing biological-process term regulation of translation. No new process is proposed, and activity is not assigned to all natural isoforms. Supporting Evidence: PMID:32989052 Ataxin-2 enhances translation of target mRNAs. |
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Download this section (compressed HTML)Q: Which sequence-verified natural ATXN2 splice products retain direct RNA binding, PABPC1/TENT2 recruitment and translation activation, given their distinct deletions and replacements?
Q: How do the RNA-binding and PABPC1-interacting regions contribute separately to transcript stabilization, translation and stress-granule assembly in human neurons?
Q: Which assay directly supports the curated ATXN2-EGFR binding assertion, and is the interaction direct or mediated through the endophilin-CIN85-Src complex?
Q: Do physiological changes in endogenous ATXN2 abundance regulate P-body assembly, or is the strong disruption mainly an overexpression-dependent effect?
Q: Which RNA cargo, if any, undergoes ATXN2-dependent directed movement independently of changes in transcript stability, translation and stress-granule partitioning?
Experiment: Compare sequence-verified natural products at matched abundance using RNA crosslinking, transcript half-life measurements, poly(A)-tail profiling and translation reporters normalized to mRNA abundance. Measure polymerase recruitment separately from catalytic output.
Experiment: Quantify stress-granule and P-body number, size and composition after graded endogenous ATXN2 depletion and rescue in human neurons, using distinct compartment markers and matched stress exposures.
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