TIA1

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0000381 regulation of alternative mRNA splicing, via spliceosome	IBA GO_REF:0000033	ACCEPT	Summary: TIA1 is extensively validated as a regulator of alternative splicing through phylogenetic inference and multiple experimental studies Reason: This is a core function of TIA1, well-supported by both IBA inference and extensive experimental evidence. TIA1 binds to U-rich sequences downstream of 5' splice sites and recruits U1 snRNP to regulate alternative splicing of multiple genes including Fas, CFTR, COL2A1, and FGFR2. Supporting Evidence: PMID:11106748 TIA-1 associates selectively with pre-mRNAs that contain 5' splice sites followed by U-rich sequences. TIA-1 binding to the U-rich stretches facilitates 5' splice site recognition by U1 snRNP. This activity is critical for activation of the weak 5' splice site of msl-2 and for modulating the choice of splice site partner in Fas. PMID:12486009 The results argue that binding of TIA-1 in the vicinity of a 5' ss helps to stabilize U1 snRNP recruitment, at least in part, via a direct interaction with U1-C, thus providing one molecular mechanism for the function of this splicing regulator. file:human/TIA1/TIA1-deep-research-falcon.md A well-established mechanistic function of TIA1 is enhancing recognition of weak 5′ splice sites through binding to downstream U-rich sequences and recruitment/assistance of U1 snRNP, specifically via the U1-C protein.
GO:0140517 protein-RNA adaptor activity	IBA GO_REF:0000033	ACCEPT	Summary: TIA1 acts as an adaptor between RNA and U1 snRNP components, bridging RNA recognition and protein recruitment Reason: This accurately captures TIA1's dual role of binding pre-mRNA via its RRM domains while simultaneously interacting with U1 snRNP components (particularly U1-C) to facilitate spliceosome assembly. This adaptor function is central to how TIA1 promotes U1 snRNP recruitment to weak splice sites. Supporting Evidence: PMID:12486009 The results argue that binding of TIA-1 in the vicinity of a 5' ss helps to stabilize U1 snRNP recruitment, at least in part, via a direct interaction with U1-C, thus providing one molecular mechanism for the function of this splicing regulator. file:human/TIA1/TIA1-deep-research-falcon.md A structural organization model also emphasizes that the C-terminal Q-rich region contributes to recruiting spliceosomal factors (U1-C) without being required for RNA binding per se.
GO:0003676 nucleic acid binding	IEA GO_REF:0000002	MODIFY	Summary: Too general; TIA1's binding specificity is better captured by more specific RNA binding terms Reason: While technically correct (TIA1 does bind nucleic acids including RNA and has been shown to bind DNA in COL2A1 genomic DNA), this term is too broad and uninformative. The more specific 'RNA binding' (GO:0003723) better represents TIA1's primary molecular function, which is extensively characterized for RNA. Note that TIA1 can also bind DNA but this appears to be a minor function. Proposed replacements: RNA binding
GO:0003723 RNA binding	IEA GO_REF:0000120	ACCEPT	Summary: Core molecular function supported by extensive experimental evidence Reason: RNA binding is a fundamental and well-characterized molecular function of TIA1, mediated primarily by RRM2 and RRM3 domains that bind uridine-rich sequences. This is supported by numerous experimental studies and is the basis for both its splicing regulatory and translational repression activities. Supporting Evidence: PMID:8576255 Both proteins selected RNAs containing one or several short stretches of uridylate residues suggesting that the two proteins have similar RNA binding specificities. file:human/TIA1/TIA1-deep-research-falcon.md At the RRM level, a consistent model emerges: - RRM2 is the dominant high-affinity, sequence-specific RNA-binding domain. - RRM3 enhances/cooperates with RRM2. - RRM1 has little intrinsic RNA-binding affinity and contributes minimally to binding in several contexts, although it can modulate selectivity/architecture in some assays.
GO:0005634 nucleus	IEA GO_REF:0000120	ACCEPT	Summary: TIA1 is predominantly nuclear under normal conditions where it regulates splicing Reason: TIA1 is primarily localized to the nucleus under steady-state conditions, excluding the nucleolus, where it performs its splicing regulatory functions. Nuclear localization is mediated by RRM2 domain and C-terminal residues 287-340. Supporting Evidence: file:human/TIA1/TIA1-deep-research-perplexity-lite.md Nucleus: Predominantly nuclear under steady-state conditions, excluding the nucleolus
GO:0005737 cytoplasm	IEA GO_REF:0000120	ACCEPT	Summary: TIA1 translocates to cytoplasm under stress conditions Reason: While predominantly nuclear, TIA1 dynamically shuttles to the cytoplasm, particularly under cellular stress conditions where it nucleates stress granules. This dual localization is critical for its function in both splicing (nuclear) and translational regulation/stress response (cytoplasmic). Supporting Evidence: file:human/TIA1/TIA1-deep-research-perplexity-lite.md Cytoplasm: Translocates to the cytoplasm during cellular stress, where it assembles into stress granules
GO:0006397 mRNA processing	IEA GO_REF:0000043	ACCEPT	Summary: Broad term encompassing TIA1's role in splicing regulation Reason: TIA1 is involved in mRNA processing through its regulation of alternative splicing. While more specific terms like 'regulation of alternative mRNA splicing, via spliceosome' are more informative, this broader term is also correct and captures TIA1's involvement in this general process.
GO:0006915 apoptotic process	IEA GO_REF:0000043	KEEP AS NON CORE	Summary: TIA1 has context-dependent roles in apoptosis: it was originally identified as inducing DNA fragmentation in cytotoxic-granule target cells and regulates Fas splicing, but in germinal center B cells it is anti-apoptotic via promotion of Mcl1 translation. Reason: TIA1's relationship to apoptosis is context-dependent rather than a single core constitutive function. It was originally identified as inducing DNA fragmentation in target cells of cytotoxic lymphocytes and regulates alternative splicing of the Fas receptor toward the membrane-bound apoptotic form (pro-apoptotic). However, falcon deep research documents an opposite, anti-apoptotic role in germinal center B cells, where TIA1/TIAL1 directly bind Mcl1 mRNA and promote MCL1 protein expression to protect cells from apoptosis. Because the direction of the effect depends on cell type and target mRNA, this broad process term is better retained as non-core; the core molecular activities (RNA binding, splicing regulation, translational control, stress granule nucleation) underlie these downstream apoptotic phenotypes. Supporting Evidence: PMID:1934064 Both natural and recombinant TIA-1 were found to induce DNA fragmentation in digitonin permeabilized thymocytes, suggesting that these molecules may be the granule components responsible for inducing apoptosis in CTL targets. PMID:11106748 We report here that the apoptosis-promoting protein TIA-1 regulates alternative pre-mRNA splicing of the Drosophila melanogaster gene male-specific-lethal 2 and of the human apoptotic gene Fas. file:human/TIA1/TIA1-deep-research-falcon.md Mechanistically, TIA1/TIAL1 directly bind Mcl1 mRNA and promote MCL1 protein expression, protecting GC B cells from apoptosis and enabling productive, high-affinity antibody responses.
GO:0008380 RNA splicing	IEA GO_REF:0000043	ACCEPT	Summary: General term for TIA1's well-established splicing function Reason: This is accurate but less specific than 'regulation of alternative mRNA splicing, via spliceosome'. TIA1 regulates RNA splicing by modulating U1 snRNP recruitment to weak 5' splice sites. The more specific term is preferable but this general term is also correct.
GO:0010494 cytoplasmic stress granule	IEA GO_REF:0000120	ACCEPT	Summary: TIA1 is a core nucleator and component of cytoplasmic stress granules Reason: This is a core cellular location and function of TIA1 under stress conditions. TIA1 nucleates stress granule assembly through its prion-like domain and recruits untranslated mRNAs to these granules, leading to stress-induced translational arrest. This is one of TIA1's most well-established functions. Supporting Evidence: file:human/TIA1/TIA1-deep-research-perplexity-lite.md Under cellular stress, TIA1 translocates to the cytoplasm and nucleates stress granules—membraneless organelles that sequester non-essential mRNAs, modulating the translational response. The prion-like domain (PLD) is critical for self-assembly and stress granule formation. file:human/TIA1/TIA1-deep-research-falcon.md TIA1 is described as a canonical SG component that can connect eIF2α phosphorylation to SG assembly and translational repression/mRNA triage during stress.
GO:0000381 regulation of alternative mRNA splicing, via spliceosome	IEA GO_REF:0000120	ACCEPT	Summary: Duplicate of earlier IBA annotation - core function of TIA1 Reason: This is a duplicate annotation (same term appears with IBA evidence). Keeping as this represents a core, well-established function of TIA1 in regulating alternative splicing through U1 snRNP recruitment.
GO:0003730 mRNA 3'-UTR binding	IEA GO_REF:0000107	ACCEPT	Summary: TIA1 binds 3'UTRs to regulate mRNA translation and stability Reason: TIA1 binds to AU-rich elements in mRNA 3'UTRs as part of its role in translational repression. This is a well-supported function distinct from its splicing activity, and represents another core molecular function of TIA1. Supporting Evidence: file:human/TIA1/TIA1-deep-research-perplexity-lite.md TIA1 binds uridine-rich (U-rich) sequences in the 3' untranslated regions (3'UTRs) and introns of target mRNAs, regulating their splicing and translation. Translational Silencing: TIA1 can inhibit translation of specific mRNAs, such as TNFα and COX-2, by binding to their U-rich elements, acting as a translational silencer.
GO:0017148 negative regulation of translation	IEA GO_REF:0000107	ACCEPT	Summary: TIA1 represses translation through 3'UTR binding and stress granule sequestration Reason: TIA1 negatively regulates translation through two mechanisms - direct translational silencing by binding AU-rich elements in 3'UTRs of target mRNAs (like TNF and PTGS2/COX-2), and indirectly by sequestering mRNAs in stress granules under stress conditions. This is a core function of TIA1 in the cytoplasm. Supporting Evidence: file:human/TIA1/TIA1-deep-research-perplexity-lite.md Translational Silencing: TIA1 can inhibit translation of specific mRNAs, such as TNFα and COX-2, by binding to their U-rich elements, acting as a translational silencer file:human/TIA1/TIA1-deep-research-falcon.md TIA1 is described as a canonical SG component that can connect eIF2α phosphorylation to SG assembly and translational repression/mRNA triage during stress.
GO:0035925 mRNA 3'-UTR AU-rich region binding	IEA GO_REF:0000107	ACCEPT	Summary: More specific term for TIA1's 3'UTR binding activity Reason: This is the most specific and accurate molecular function term for TIA1's 3'UTR binding activity. TIA1 specifically recognizes and binds AU-rich (uridine-rich) elements in mRNA 3'UTRs to regulate translation. This specificity is what distinguishes TIA1 from general RNA-binding proteins.
GO:0097165 nuclear stress granule	IEA GO_REF:0000120	ACCEPT	Summary: TIA1 can localize to nuclear stress granules in addition to cytoplasmic ones Reason: While TIA1 is best known for nucleating cytoplasmic stress granules, it can also form nuclear stress granules under certain stress conditions. This represents the full range of TIA1's stress granule localization. Supporting Evidence: file:human/TIA1/TIA1-deep-research-perplexity-lite.md Dynamic Shuttling: Nuclear import is mediated by the RRM2 domain and the N-terminal region of the Q/N-rich domain, via a Ran-GTP and CRM1-dependent pathway.
GO:0005515 protein binding	IPI PMID:12486009 The splicing regulator TIA-1 interacts with U1-C to promote ...	MODIFY	Summary: Non-informative general term; TIA1's specific protein interactions are better captured by other terms Reason: While technically correct that TIA1 binds proteins (particularly U1-C, FASTK, and other spliceosomal components), this term is too general and uninformative per curation guidelines. The 'protein-RNA adaptor activity' term better captures TIA1's functionally relevant protein interactions in the context of its RNA-binding activity. Proposed replacements: protein-RNA adaptor activity Supporting Evidence: PMID:12486009 Co-precipitation experiments revealed a specific and direct interaction involving the N-terminal region of the U1 protein U1-C and the Q-rich domain of TIA-1
GO:0005654 nucleoplasm	IDA GO_REF:0000052	ACCEPT	Summary: More specific nuclear localization based on immunofluorescence data Reason: TIA1 localizes specifically to the nucleoplasm (excluding nucleolus) under normal conditions. This is more specific than the general 'nucleus' term and is supported by experimental localization data.
GO:0005829 cytosol	IDA GO_REF:0000052	ACCEPT	Summary: Specific cytoplasmic compartment where TIA1 functions under stress Reason: TIA1 localizes to the cytosol when it translocates from the nucleus, particularly under stress conditions. This is more specific than general 'cytoplasm' and accurately represents TIA1's cytoplasmic localization.
GO:0000381 regulation of alternative mRNA splicing, via spliceosome	IDA PMID:14966131 An intronic polypyrimidine-rich element downstream of the do...	ACCEPT	Summary: Direct experimental evidence for TIA1 regulating CFTR exon 9 alternative splicing Reason: This study demonstrates TIA1's role in promoting CFTR exon 9 inclusion by binding to polypyrimidine-rich elements downstream of the weak 5' splice site, providing direct evidence for a core function. Supporting Evidence: PMID:14966131 An intronic polypyrimidine-rich element downstream of the donor site modulates cystic fibrosis transmembrane conductance regulator exon 9 alternative splicing
GO:0000381 regulation of alternative mRNA splicing, via spliceosome	IDA PMID:17580305 Nuclear protein TIA-1 regulates COL2A1 alternative splicing ...	ACCEPT	Summary: Direct experimental evidence for TIA1 regulating COL2A1 alternative splicing Reason: This study shows TIA1 binds to AU-rich elements in COL2A1 intron 2 and regulates alternative splicing of exon 2, providing specific experimental validation of TIA1's splicing regulatory function. Supporting Evidence: PMID:17580305 Nuclear protein TIA-1 regulates COL2A1 alternative splicing and interacts with precursor mRNA and genomic DNA
GO:0003723 RNA binding	IDA PMID:8576255 Individual RNA recognition motifs of TIA-1 and TIAR have dif...	ACCEPT	Summary: Foundational study characterizing TIA1's RNA binding specificity Reason: This is the key study that defined TIA1's RNA binding specificity, showing that RRM2 is necessary and sufficient for binding uridylate-rich sequences. Essential evidence for TIA1's core molecular function. Supporting Evidence: PMID:8576255 Both proteins selected RNAs containing one or several short stretches of uridylate residues suggesting that the two proteins have similar RNA binding specificities.
GO:0003730 mRNA 3'-UTR binding	ISS GO_REF:0000024	ACCEPT	Summary: Inferred from ortholog studies, consistent with TIA1's characterized function Reason: While inferred by sequence similarity to orthologs, this is consistent with well-established direct evidence showing TIA1 binds 3'UTRs to regulate translation. The ISS annotation is valid and supported by experimental evidence in the human protein.
GO:0005515 protein binding	IPI PMID:17135269 Fas-activated serine/threonine kinase (FAST K) synergizes wi...	MODIFY	Summary: Non-informative general term despite experimental evidence Reason: This study shows specific interaction with FASTK, but the generic 'protein binding' term is not informative per curation guidelines. The protein-RNA adaptor activity term better captures functionally relevant protein interactions. Proposed replacements: protein-RNA adaptor activity Supporting Evidence: PMID:17135269 2006 Nov 29. Fas-activated serine/threonine kinase (FAST K) synergizes with TIA-1/TIAR proteins to regulate Fas alternative splicing.
GO:0005634 nucleus	IDA PMID:8576255 Individual RNA recognition motifs of TIA-1 and TIAR have dif...	ACCEPT	Summary: Direct experimental observation of nuclear localization Reason: Early foundational study demonstrating TIA1's nuclear localization, which is where it performs its splicing regulatory functions. Supporting Evidence: PMID:8576255 Individual RNA recognition motifs of TIA-1 and TIAR have different RNA binding specificities.
GO:0005737 cytoplasm	IDA PMID:7488725 Rapid habituation of auditory responses of locus coeruleus c...	ACCEPT	Summary: Direct observation of cytoplasmic localization Reason: Direct experimental evidence for TIA1's cytoplasmic localization, particularly relevant for its stress granule and translational regulatory functions. Supporting Evidence: PMID:7488725 Rapid habituation of auditory responses of locus coeruleus cells in anaesthetized and awake rats.
GO:0010494 cytoplasmic stress granule	IDA PMID:8576255 Individual RNA recognition motifs of TIA-1 and TIAR have dif...	ACCEPT	Summary: Foundational study on TIA1's stress granule localization Reason: This key study demonstrated TIA1's localization to stress granules, establishing one of TIA1's most important cellular functions. Supporting Evidence: PMID:8576255 Individual RNA recognition motifs of TIA-1 and TIAR have different RNA binding specificities.
GO:0017148 negative regulation of translation	ISS GO_REF:0000024	ACCEPT	Summary: Inferred from orthologs but well-supported by direct evidence in human Reason: While annotated by sequence similarity, TIA1's role in translational repression is well-established in human through direct studies showing it silences translation of TNF, COX-2, and other ARE-containing mRNAs.
GO:0034063 stress granule assembly	IDA PMID:8576255 Individual RNA recognition motifs of TIA-1 and TIAR have dif...	ACCEPT	Summary: Core function - TIA1 nucleates stress granule assembly Reason: This is one of TIA1's most important and well-characterized biological process functions. TIA1 nucleates stress granule assembly through its prion-like domain, which is essential for the stress response. Supporting Evidence: file:human/TIA1/TIA1-deep-research-perplexity-lite.md The prion-like domain (PLD) is critical for self-assembly and stress granule formation, and is implicated in disease-associated aggregation PMID:8576255 Individual RNA recognition motifs of TIA-1 and TIAR have different RNA binding specificities. file:human/TIA1/TIA1-deep-research-falcon.md The C-terminal low-complexity/prion-like domain is a major determinant of condensation/LLPS and SG assembly.
GO:0048024 regulation of mRNA splicing, via spliceosome	IDA PMID:7488725 Rapid habituation of auditory responses of locus coeruleus c...	ACCEPT	Summary: Broader splicing regulation term encompassing alternative splicing Reason: This is a broader term that encompasses TIA1's splicing regulatory activity. While 'regulation of alternative mRNA splicing, via spliceosome' is more specific, this general term is also correct. Supporting Evidence: PMID:7488725 Rapid habituation of auditory responses of locus coeruleus cells in anaesthetized and awake rats.
GO:0005515 protein binding	IPI PMID:18164289 Dual localization of the RNA binding protein CUGBP-1 to stre...	MODIFY	Summary: Non-informative general term Reason: Another instance of the overly general 'protein binding' term. While TIA1 does interact with proteins, this term provides no functional insight. The protein-RNA adaptor activity term is more informative. Proposed replacements: protein-RNA adaptor activity Supporting Evidence: PMID:18164289 2007 Nov 12. Dual localization of the RNA binding protein CUGBP-1 to stress granule and perinucleolar compartment.
GO:0005634 nucleus	IDA PMID:18164289 Dual localization of the RNA binding protein CUGBP-1 to stre...	ACCEPT	Summary: Additional experimental confirmation of nuclear localization Reason: Another study confirming TIA1's nuclear localization under normal conditions. Supporting Evidence: PMID:18164289 2007 Nov 12. Dual localization of the RNA binding protein CUGBP-1 to stress granule and perinucleolar compartment.
GO:0010494 cytoplasmic stress granule	ISS GO_REF:0000024	ACCEPT	Summary: Inferred from orthologs but strongly supported by direct evidence Reason: While inferred by sequence similarity, TIA1's localization to and nucleation of cytoplasmic stress granules is one of its most well-established functions with extensive direct experimental support.
GO:0005737 cytoplasm	IDA PMID:24965446 Host factors that interact with the pestivirus N-terminal pr...	ACCEPT	Summary: Recent experimental confirmation of cytoplasmic localization Reason: Recent study confirming TIA1's cytoplasmic localization, particularly in the context of viral infection and stress granule formation. Supporting Evidence: PMID:24965446 Host factors that interact with the pestivirus N-terminal protease, Npro, are components of the ribonucleoprotein complex.
GO:1903608 protein localization to cytoplasmic stress granule	IMP PMID:24965446 Host factors that interact with the pestivirus N-terminal pr...	ACCEPT	Summary: TIA1 actively directs proteins to stress granules Reason: This term captures an important aspect of TIA1's function - not just that it localizes to stress granules itself, but that it actively recruits other proteins and mRNAs to stress granules. This mutant phenotype evidence demonstrates TIA1's active role in organizing stress granule composition. Supporting Evidence: PMID:24965446 Host factors that interact with the pestivirus N-terminal protease, Npro, are components of the ribonucleoprotein complex.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-6803527	ACCEPT	Summary: Reactome pathway annotation for nucleoplasm localization Reason: Traceable author statement from Reactome pathway database confirming TIA1's nucleoplasm localization in the context of FGFR2 alternative splicing regulation.
GO:0003723 RNA binding	HDA PMID:22658674 Insights into RNA biology from an atlas of mammalian mRNA-bi...	ACCEPT	Summary: Large-scale proteomics study identifying TIA1 as mRNA-binding protein Reason: High-throughput direct assay providing independent confirmation of TIA1's RNA binding activity through proteome-wide mRNA-binding protein analysis. Supporting Evidence: PMID:22658674 May 31. Insights into RNA biology from an atlas of mammalian mRNA-binding proteins.
GO:0003723 RNA binding	HDA PMID:22681889 The mRNA-bound proteome and its global occupancy profile on ...	ACCEPT	Summary: Another large-scale proteomics confirmation of RNA binding Reason: Independent high-throughput study confirming TIA1 as an mRNA-bound protein, providing additional proteome-wide evidence for this core function. Supporting Evidence: PMID:22681889 The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts.
GO:0010494 cytoplasmic stress granule	IDA PMID:21984414 The RNA recognition motif protein RBM11 is a novel tissue-sp...	ACCEPT	Summary: Additional direct experimental evidence for stress granule localization Reason: Further direct experimental confirmation of TIA1's cytoplasmic stress granule localization. Supporting Evidence: PMID:21984414 Oct 7. The RNA recognition motif protein RBM11 is a novel tissue-specific splicing regulator.
GO:0097165 nuclear stress granule	IDA PMID:21984414 The RNA recognition motif protein RBM11 is a novel tissue-sp...	ACCEPT	Summary: Direct experimental evidence for nuclear stress granule localization Reason: This study provides direct experimental evidence that TIA1 can form or localize to nuclear stress granules in addition to the more commonly studied cytoplasmic stress granules. Supporting Evidence: PMID:21984414 Oct 7. The RNA recognition motif protein RBM11 is a novel tissue-specific splicing regulator.
GO:0005515 protein binding	IPI PMID:7544399 Fas-activated serine/threonine kinase (FAST) phosphorylates ...	MODIFY	Summary: Non-informative general term from FASTK interaction study Reason: This study demonstrates TIA1 interaction with FASTK kinase, but the generic 'protein binding' term is uninformative. The protein-RNA adaptor activity better captures TIA1's functionally relevant protein interactions. Proposed replacements: protein-RNA adaptor activity Supporting Evidence: PMID:7544399 In response to Fas ligation, it is rapidly dephosphorylated and concomitantly activated to phosphorylate TIA-1, a nuclear RNA-binding protein that has been implicated as an effector of apoptosis.
GO:0048024 regulation of mRNA splicing, via spliceosome	IDA PMID:11106748 The apoptosis-promoting factor TIA-1 is a regulator of alter...	ACCEPT	Summary: Landmark study establishing TIA1 as splicing regulator Reason: This is the seminal paper demonstrating TIA1's role as a regulator of alternative splicing, showing it promotes U1 snRNP recruitment to weak 5' splice sites. Essential evidence for this core function. Supporting Evidence: PMID:11106748 TIA-1 associates selectively with pre-mRNAs that contain 5' splice sites followed by U-rich sequences. TIA-1 binding to the U-rich stretches facilitates 5' splice site recognition by U1 snRNP.
GO:0006915 apoptotic process	TAS PMID:1934064 A polyadenylate binding protein localized to the granules of...	KEEP AS NON CORE	Summary: Original paper identifying TIA1 as apoptosis-inducing protein Reason: This is the original 1991 paper that discovered TIA1 and showed it induces DNA fragmentation and apoptosis in target cells of cytotoxic lymphocytes. This is context-specific rather than constitutive: falcon deep research notes that in other settings (germinal center B cells) TIA1 is instead anti-apoptotic via Mcl1 translation, so the apoptosis relationship is cell-type dependent. The original cytotoxic-lymphocyte function nonetheless represents an important documented role, retained here as non-core consistent with the other apoptotic_process annotation. Supporting Evidence: PMID:1934064 Both natural and recombinant TIA-1 were found to induce DNA fragmentation in digitonin permeabilized thymocytes, suggesting that these molecules may be the granule components responsible for inducing apoptosis in CTL targets. file:human/TIA1/TIA1-deep-research-falcon.md Mechanistically, TIA1/TIAL1 directly bind Mcl1 mRNA and promote MCL1 protein expression, protecting GC B cells from apoptosis and enabling productive, high-affinity antibody responses.
GO:0008143 poly(A) binding	TAS PMID:1934064 A polyadenylate binding protein localized to the granules of...	ACCEPT	Summary: Early characterization as poly(A) binding protein Reason: The original paper characterized TIA1 as a polyadenylate-binding protein based on sequence similarity to poly(A)-binding proteins. While TIA1's binding is more accurately described as U-rich/AU-rich element binding, it can bind poly(A) sequences and this represents the historical characterization of the protein. Supporting Evidence: PMID:1934064 A polyadenylate binding protein localized to the granules of cytolytic lymphocytes induces DNA fragmentation in target cells.

Gene Description

Existing Annotations Review

Core Functions

Promoting U1 snRNP recruitment to weak 5' splice sites containing downstream U-rich sequences to facilitate alternative exon inclusion

Nucleating stress granule assembly through prion-like domain-mediated phase separation to sequester untranslated mRNAs during cellular stress

Repressing translation by binding AU-rich elements in mRNA 3' UTRs to silence specific mRNAs

References

Deep Research

Falcon

Perplexity

📚 Additional Documentation

Annotation Breakdown

Curation Complete

Curation Summary

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