WHI3

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0000932 P-body	IDA PMID:24386402 Effects of the yeast RNA-binding protein Whi3 on the half-li...	KEEP AS NON CORE	Summary: Whi3-GFP forms cytoplasmic foci that co-localize with P-body and stress-granule markers after glucose depletion or heat shock. Reason: Direct imaging (IDA) in Cai & Futcher supports P-body localization under stress. The authors did not rigorously separate P-bodies from stress granules, and Whi3 is diffuse and active in unstressed cells, so this stress-induced location is peripheral to its core mRNA-regulatory function. Supporting Evidence: PMID:24386402 Under stress conditions, Whi3 becomes a component of P-bodies or stress granules, but Whi3 also acts under non-stress condition, when no P-bodies are visible
GO:0001403 invasive growth in response to glucose limitation	IMP PMID:14685274 Recruitment of Cdc28 by Whi3 restricts nuclear accumulation ...	KEEP AS NON CORE	Summary: whi3 mutants are defective for filamentous/invasive growth; the Whi3 N-terminal Cdc28-binding domain is required for filamentous growth. Reason: SGD experimental annotation from the Wang et al. EMBO J paper, whose full text reports a role for the Whi3 N-terminal domain in filamentous growth. Invasive growth is a developmental output of Whi3's control of G1 cyclin-Cdk and of Yak1/Tec1/FLO11, not its core activity, so it is kept as non-core. The specific glucose-limitation assay is not visible in the cached text; defer to the curator. Supporting Evidence: PMID:14685274 Efficient interaction with Cdc28 depends on an N-terminal domain of Whi3 that is also required for cytoplasmic localization of Cdc28, and for proper regulation of G1 length and filamentous growth PMID:11691832 Whi3 is also required for restraining Cln3 function in meiosis, filamentation, and mating
GO:0003676 nucleic acid binding	IEA GO_REF:0000002	MODIFY	Summary: InterPro RBD-domain superfamily mapping to nucleic acid binding. Reason: Correct but too general: Whi3 has a canonical RRM and binds specific mRNAs (CLN3 and hundreds of GCAU-rich targets) experimentally, so the supported descendant is mRNA binding (GO:0003729), which the gene already carries. Proposed replacements: mRNA binding Supporting Evidence: file:yeast/WHI3/WHI3-uniprot.txt DR Pfam; PF00076; RRM_1; 1. PMID:11691832 Whi3 contains an RNA-recognition motif that specifically binds the CLN3 mRNA
GO:0003723 RNA binding	IEA GO_REF:0000002	MODIFY	Summary: InterPro RRM-domain mapping to RNA binding. Reason: Correct but less specific than the evidence: RIP-chip and in vitro binding show Whi3 binds mRNAs, so refine to mRNA binding (GO:0003729), already carried by the gene. Proposed replacements: mRNA binding Supporting Evidence: file:yeast/WHI3/WHI3-uniprot.txt DR Pfam; PF00076; RRM_1; 1. PMID:18667435 Whi3-associated mRNAs are enriched in clusters of the tetranucleotide GCAU, and mutation of the GCAU clusters in the CLN3 mRNA caused a reduction in its association to Whi3
GO:0003729 mRNA binding	IBA GO_REF:0000033	ACCEPT	Summary: PAINT IBA for mRNA binding; WHI3 (SGD:S000005141) is among the experimentally annotated descendants. Reason: Consistent with direct experimental evidence for Whi3 binding CLN3 and many other mRNAs; Whi3 appearing in its own WITH/FROM reflects its own experimental grounding. Supporting Evidence: PMID:11691832 Whi3 contains an RNA-recognition motif that specifically binds the CLN3 mRNA PMID:18667435 Whi3-associated mRNAs are enriched in clusters of the tetranucleotide GCAU, and mutation of the GCAU clusters in the CLN3 mRNA caused a reduction in its association to Whi3
GO:0003729 mRNA binding	IDA PMID:11691832 Whi3 binds the mRNA of the G1 cyclin CLN3 to modulate cell f...	ACCEPT	Summary: Gari et al. showed the Whi3 RRM specifically binds CLN3 mRNA and that RRM mutation abolishes function. Reason: Core molecular function: sequence-specific binding of the CLN3 mRNA, confirmed by later RIP-chip studies mapping GCAU motifs. Supporting Evidence: PMID:11691832 Whi3 contains an RNA-recognition motif that specifically binds the CLN3 mRNA PMID:18667435 Whi3-associated mRNAs are enriched in clusters of the tetranucleotide GCAU, and mutation of the GCAU clusters in the CLN3 mRNA caused a reduction in its association to Whi3
GO:0003729 mRNA binding	IDA PMID:24386402 Effects of the yeast RNA-binding protein Whi3 on the half-li...	ACCEPT	Summary: RIP-chip of Whi3-TAP versus RRM-deleted Whi3 identified 111 bound mRNAs including CLN3. Reason: Direct RNA immunoprecipitation evidence for mRNA binding; core function. Supporting Evidence: PMID:18667435 Whi3-associated mRNAs are enriched in clusters of the tetranucleotide GCAU, and mutation of the GCAU clusters in the CLN3 mRNA caused a reduction in its association to Whi3 PMID:24386402 the whi3 mutation causes a small but consistent increase in the abundance of hundreds of mRNAs, including the CLN3 mRNA
GO:0003729 mRNA binding	IMP PMID:11691832 Whi3 binds the mRNA of the G1 cyclin CLN3 to modulate cell f...	ACCEPT	Summary: Gari et al. showed the Whi3 RRM specifically binds CLN3 mRNA and that RRM mutation abolishes function. Reason: Core molecular function: sequence-specific binding of the CLN3 mRNA, confirmed by later RIP-chip studies mapping GCAU motifs. Supporting Evidence: PMID:11691832 Whi3 contains an RNA-recognition motif that specifically binds the CLN3 mRNA PMID:18667435 Whi3-associated mRNAs are enriched in clusters of the tetranucleotide GCAU, and mutation of the GCAU clusters in the CLN3 mRNA caused a reduction in its association to Whi3
GO:0005515 protein binding	IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine...	REMOVE	Summary: Interaction with Ssa2 (Hsp70) from a high-throughput affinity purification. Reason: Bare GO:0005515 protein binding is uninformative under the project protein-binding policy and is removed; removal does not mean the reported interaction is false. The Ssa2 (Hsp70) interaction is plausible (Hsp70 counteracts Whi3 super-assembly; Whi4 is the partially redundant paralogue), but no more informative MF term is supported by this paper.
GO:0005515 protein binding	IPI PMID:31454312 The role of structural pleiotropy and regulatory evolution i...	REMOVE	Summary: Interaction with Whi4 (paralogue) from a paralogue heteromer study. Reason: Bare GO:0005515 protein binding is uninformative under the project protein-binding policy and is removed; removal does not mean the reported interaction is false. The Whi4 (paralogue) interaction is plausible (Hsp70 counteracts Whi3 super-assembly; Whi4 is the partially redundant paralogue), but no more informative MF term is supported by this paper.
GO:0005515 protein binding	IPI PMID:37968396 The social and structural architecture of the yeast protein ...	REMOVE	Summary: Interaction with Ssa2 (Hsp70) from a high-throughput affinity purification. Reason: Bare GO:0005515 protein binding is uninformative under the project protein-binding policy and is removed; removal does not mean the reported interaction is false. The Ssa2 (Hsp70) interaction is plausible (Hsp70 counteracts Whi3 super-assembly; Whi4 is the partially redundant paralogue), but no more informative MF term is supported by this paper.
GO:0005515 protein binding	IPI PMID:37968396 The social and structural architecture of the yeast protein ...	REMOVE	Summary: Interaction with Whi4 (paralogue) from a high-throughput affinity purification. Reason: Bare GO:0005515 protein binding is uninformative under the project protein-binding policy and is removed; removal does not mean the reported interaction is false. The Whi4 (paralogue) interaction is plausible (Hsp70 counteracts Whi3 super-assembly; Whi4 is the partially redundant paralogue), but no more informative MF term is supported by this paper.
GO:0005737 cytoplasm	IDA PMID:11691832 Whi3 binds the mRNA of the G1 cyclin CLN3 to modulate cell f...	ACCEPT	Summary: Whi3 localizes the CLN3 mRNA into discrete cytoplasmic foci; Whi3 is cytoplasmic. Reason: Cytoplasmic localization is supported by several independent studies (diffuse cytoplasmic Whi3-GFP in unstressed cells, cytoplasmic retention of Cln3-Cdc28), and is where Whi3 regulates its target mRNAs. Supporting Evidence: PMID:11691832 localizes the CLN3 mRNA into discrete cytoplasmic foci PMID:14685274 We propose that Whi3 constitutes a cytoplasmic retention device for Cln3-Cdc28 complexes
GO:0005789 endoplasmic reticulum membrane	IDA PMID:35085498 Whi3 mnemon association with endoplasmic reticulum membranes...	ACCEPT	Summary: Whi3 mnemon super-assemblies lie on Sec61-marked ER membranes and Whi3-TAP partly co-fractionates with Dpm1-positive microsomes. Reason: Two independent assays (imaging against an ER membrane marker and microsome co-fractionation) in Lau et al., agreeing with earlier reports of ER association (Colomina et al. 2008). Whi3 has no TM segment, so this is peripheral membrane association, which located_in covers. The ER association underlies both Cln3 retention and the mother-confined memory. Supporting Evidence: PMID:35085498 Accordingly, Whi3 partly cofractionated with the microsomes in the lysates of cells before and after pheromone treatment PMID:35085498 Here, we report that Whi3mnem is closely associated with endoplasmic reticulum (ER) membranes and is retained in the mother cell by the lateral diffusion barriers present at the bud neck
GO:0007089 traversing start control point of mitotic cell cycle	IGI PMID:11691832 Whi3 binds the mRNA of the G1 cyclin CLN3 to modulate cell f...	MODIFY	Summary: IGI with CLN3: whi3 cells pass Start at a smaller size; Whi3 restrains Cln3 function at the G1/S transition. Reason: Whi3 acts as a dose-dependent inhibitor of Start, not as a component that drives traversal. The sign-correct term is negative regulation of G1/S transition of mitotic cell cycle (GO:2000134). The genetic data (whi3 small, extra WHI3 large or G1-arrested, CLN3 epistasis) are sound, so this is a lateral correction, not a removal. Proposed replacements: negative regulation of G1/S transition of mitotic cell cycle Supporting Evidence: PMID:11691832 Here we show that Whi3 is a negative regulator of Cln3, a G1 cyclin that promotes transcription of many genes to trigger the G1/S transition in budding yeast PMID:11290704 The whi3 mutant has small cells, while extra doses of WHI3 produce large cells, and a large excess of WHI3 produces a lethal arrest in G1 phase. WHI3 seems to be a dose-dependent inhibitor of Start.
GO:0007089 traversing start control point of mitotic cell cycle	IMP PMID:11691832 Whi3 binds the mRNA of the G1 cyclin CLN3 to modulate cell f...	MODIFY	Summary: whi3 cells pass Start at a smaller size; Whi3 restrains Cln3 function at the G1/S transition. Reason: Whi3 acts as a dose-dependent inhibitor of Start, not as a component that drives traversal. The sign-correct term is negative regulation of G1/S transition of mitotic cell cycle (GO:2000134). The genetic data (whi3 small, extra WHI3 large or G1-arrested, CLN3 epistasis) are sound, so this is a lateral correction, not a removal. Proposed replacements: negative regulation of G1/S transition of mitotic cell cycle Supporting Evidence: PMID:11691832 Here we show that Whi3 is a negative regulator of Cln3, a G1 cyclin that promotes transcription of many genes to trigger the G1/S transition in budding yeast PMID:11290704 The whi3 mutant has small cells, while extra doses of WHI3 produce large cells, and a large excess of WHI3 produces a lethal arrest in G1 phase. WHI3 seems to be a dose-dependent inhibitor of Start.
GO:0007124 pseudohyphal growth	IMP PMID:14685274 Recruitment of Cdc28 by Whi3 restricts nuclear accumulation ...	KEEP AS NON CORE	Summary: whi3 mutants block filamentous (pseudohyphal) growth. Reason: Supported by the dfg transposon screen and by Wang et al.; pseudohyphal growth is a developmental output of Whi3's post-transcriptional control of G1 cyclins and FLO11 regulators, so it is kept as non-core. Supporting Evidence: PMID:14685274 Efficient interaction with Cdc28 depends on an N-terminal domain of Whi3 that is also required for cytoplasmic localization of Cdc28, and for proper regulation of G1 length and filamentous growth
GO:0007124 pseudohyphal growth	IMP PMID:9055077 Dissection of filamentous growth by transposon mutagenesis i...	KEEP AS NON CORE	Summary: whi3 mutants block filamentous (pseudohyphal) growth. Reason: Supported by the dfg transposon screen and by Wang et al.; pseudohyphal growth is a developmental output of Whi3's post-transcriptional control of G1 cyclins and FLO11 regulators, so it is kept as non-core. Supporting Evidence: PMID:9055077 we thereby identified 16 different genes, CDC39, STE12, TEC1, WHI3, NAB1, DBR1, CDC55, SRV2, TPM1, SPA2, BNI1, DFG5, DFG9, DFG10, BUD8 and DFG16, mutations that block filamentous growth
GO:0008361 regulation of cell size	HMP PMID:12089449 Systematic identification of pathways that couple cell growt...	MODIFY	Summary: Genome-wide cell size screen of deletion mutants: whi3 cells are small. Reason: True but general: the direction is known. whi3 cells are small and extra WHI3 makes large cells, so the specific descendant is positive regulation of cell size (GO:0045793), which the gene already carries. Proposed replacements: positive regulation of cell size Supporting Evidence: PMID:11290704 The whi3 mutant has small cells, while extra doses of WHI3 produce large cells, and a large excess of WHI3 produces a lethal arrest in G1 phase. WHI3 seems to be a dose-dependent inhibitor of Start.
GO:0008361 regulation of cell size	IEA GO_REF:0000117	MODIFY	Summary: ARBA rule mapping: whi3 cells are small. Reason: True but general: the direction is known. whi3 cells are small and extra WHI3 makes large cells, so the specific descendant is positive regulation of cell size (GO:0045793), which the gene already carries. Proposed replacements: positive regulation of cell size Supporting Evidence: PMID:11290704 The whi3 mutant has small cells, while extra doses of WHI3 produce large cells, and a large excess of WHI3 produces a lethal arrest in G1 phase. WHI3 seems to be a dose-dependent inhibitor of Start.
GO:0010494 cytoplasmic stress granule	HDA PMID:26777405 ATPase-Modulated Stress Granules Contain a Diverse Proteome ...	KEEP AS NON CORE	Summary: Whi3 identified in the purified yeast stress-granule core proteome. Reason: High-throughput proteomic identification (Whi3 is not named in the cached main text; it is presumably in the supplementary tables), corroborated by direct imaging in Holmes et al. and Cai & Futcher. Stress-granule recruitment is a stress-specific location, peripheral to the core function. Supporting Evidence: PMID:24386330 We show that Whi3 localizes to stress granules in response to glucose deprivation or heat shock
GO:0010494 cytoplasmic stress granule	IDA PMID:24386330 Whi3, an S. cerevisiae RNA-binding protein, is a component o...	KEEP AS NON CORE	Summary: Whi3-GFP co-localizes with Pub1 in stress granules after heat shock or glucose deprivation and shifts to the insoluble fraction. Reason: Direct, well-controlled evidence; kept as non-core because Whi3 functions in unstressed cells too. Supporting Evidence: PMID:24386330 We show that Whi3 localizes to stress granules in response to glucose deprivation or heat shock
GO:0010494 cytoplasmic stress granule	IDA PMID:24386402 Effects of the yeast RNA-binding protein Whi3 on the half-li...	KEEP AS NON CORE	Summary: Whi3-GFP forms foci with Pub1-mCherry after heat shock. Reason: Independent confirmation of stress-granule localization; stress-specific location peripheral to the core function. Supporting Evidence: PMID:24386402 Under stress conditions, Whi3 becomes a component of P-bodies or stress granules, but Whi3 also acts under non-stress condition, when no P-bodies are visible
GO:0010811 positive regulation of cell-substrate adhesion	IMP PMID:21149646 The Yak1 protein kinase lies at the center of a regulatory c...	KEEP AS NON CORE	Summary: CACAO. Malcher et al.: whi3 deletion causes complete loss of agar adhesion (Fig. 1B), with FLO11 transcript down >7-fold; PGK1-driven FLO11 restores adhesion, and high-copy YAK1 suppresses the defect. Reason: CACAO row. What the paper shows for WHI3 (PMC full text, Fig. 1 and 2): wash-test adhesion of a whi3 deletion strain in the Sigma1278b background is lost and restored by FLO11 or YAK1 overexpression. The term matches the assay (agar adhesion is cell-substrate adhesion), so it is supported, but it is a downstream phenotype: Whi3 acts post-transcriptionally on Yak1 and Tec1, which control FLO11. Kept as a true but non-core developmental output. Supporting Evidence: PMID:21149646 we present evidence that Whi3 and Yak1 form part of a signaling pathway that regulates FLO11-mediated surface adhesion and is involved in stress resistance
GO:0045727 positive regulation of translation	IMP PMID:21149646 The Yak1 protein kinase lies at the center of a regulatory c...	MARK AS OVER ANNOTATED	Summary: CACAO. Malcher et al.: in whi3 cells Yak1-HA and GFP-Yak1 protein fall about threefold while YAK1 mRNA is unchanged (Fig. 3). Reason: CACAO row. The paper shows a post-transcriptional decrease of Yak1 protein in whi3 mutants (immunoblot plus transcript quantification, Fig. 3A-C). It does not measure translation (no polysome, ribosome-profiling or reporter-translation assay), so it cannot distinguish translation from protein stability. The authors note that YAK1 mRNA was not found among Whi3-bound mRNAs and that the effect may be indirect. Translation as a general process is therefore a stronger claim than the data: wrong granularity / phenotype read as process. Where Whi3's effect on translation has been measured directly (CLN3), it is inhibitory. Supporting Evidence: PMID:21149646 Our study further suggests that Whi3 controls YAK1 expression at the post-transcriptional level and that Yak1 targets the transcriptional regulators Sok2 and Phd1 to control FLO11 PMID:24386402 In addition, the whi3 mutation causes a small increase in the translational efficiency of CLN3 mRNA
GO:0045793 positive regulation of cell size	IMP PMID:23770701 The RNA-binding protein Whi3 is a key regulator of developme...	ACCEPT	Summary: CACAO. Schladebeck & Mosch: deletion of WHI3 significantly decreases average cell size by Coulter counter and microscopy (Fig. 1A). Reason: CACAO row. The assay (Coulter counter particle volume of whi3 vs WT, Fig. 1A, PMC full text) directly matches the term, and agrees with the original whi3 dose-dependent size phenotype (Nash et al.). Cell size is the defining readout of Whi3's Start-inhibitor function, so the term is accepted at the right granularity and direction. Supporting Evidence: PMID:11290704 The whi3 mutant has small cells, while extra doses of WHI3 produce large cells, and a large excess of WHI3 produces a lethal arrest in G1 phase. WHI3 seems to be a dose-dependent inhibitor of Start.
GO:0045893 positive regulation of DNA-templated transcription	IMP PMID:21149646 The Yak1 protein kinase lies at the center of a regulatory c...	MARK AS OVER ANNOTATED	Summary: CACAO. Malcher et al.: FLO11 transcript levels drop >7-fold and a PFLO11-lacZ reporter drops >6-fold in whi3 cells (Fig. 1A, C). Reason: CACAO row: phenotype read as process. The paper shows reduced FLO11 promoter output in a whi3 deletion, but Whi3 is a cytoplasmic RNA-binding protein; the authors place it upstream of Yak1, which acts on Sok2, Phd1 and Haa1, the transcription factors on the FLO11 promoter. Whi3 does no part of transcription, and the effect is several steps downstream. Not removed, because the measured promoter dependency is real. Supporting Evidence: PMID:21149646 Our study further suggests that Whi3 controls YAK1 expression at the post-transcriptional level and that Yak1 targets the transcriptional regulators Sok2 and Phd1 to control FLO11
GO:0045901 positive regulation of translational elongation	IMP PMID:23770701 The RNA-binding protein Whi3 is a key regulator of developme...	MARK AS OVER ANNOTATED	Summary: CACAO. Schladebeck & Mosch: whi3 cells are hypersensitive to geneticin and hygromycin B and slightly to cycloheximide (Fig. 3). Reason: CACAO row: phenotype read as process. The only evidence (PMC full text, Fig. 3) is spot-assay sensitivity to elongation inhibitors, which the authors interpret as 'suggesting that Whi3 might positively affect this process'. Drug hypersensitivity is indirect (it can arise from cell wall, membrane or stress defects, which whi3 cells have), and no elongation rate, polysome or ribosome transit measurement was made. Direct ribosome profiling (Cai & Futcher) shows only a small effect on CLN3 translation, in the opposite direction. Supporting Evidence: PMID:23770701 We also provide evidence that Whi3 regulates production of these factors by post-transcriptional control and might exert this function by affecting translational elongation PMID:24386402 In addition, the whi3 mutation causes a small increase in the translational efficiency of CLN3 mRNA
GO:0061013 regulation of mRNA catabolic process	IMP PMID:24386330 Whi3, an S. cerevisiae RNA-binding protein, is a component o...	MODIFY	Summary: Holmes et al.: whi3 deletion increases the relative abundance of Whi3 target mRNAs (including CLN3), with or without heat shock. Reason: Correct but general. The direction and mechanism are known from half-life measurements (Cai & Futcher), so refine to mRNA destabilization (GO:0061157), a descendant the gene already carries. Holmes et al. measured abundance only, which is consistent with this. Proposed replacements: mRNA destabilization Supporting Evidence: PMID:24386330 Deletion of Whi3 resulted in an increase in the relative abundance of Whi3 target RNAs, either in the presence or absence of heat shock PMID:24386402 the whi3 mutation causes a small but consistent increase in the abundance of hundreds of mRNAs, including the CLN3 mRNA
GO:0061157 mRNA destabilization	IEA GO_REF:0000117	ACCEPT	Summary: ARBA rule mapping to mRNA destabilization. Reason: Consistent with experimental evidence that Whi3 shortens CLN3 mRNA half-life and lowers abundance of GCAU-rich targets. Supporting Evidence: PMID:24386402 the whi3 mutation causes a small but consistent increase in the abundance of hundreds of mRNAs, including the CLN3 mRNA PMID:24386402 We suggest that Whi3 may be a very broadly-acting, but mild, modulator of mRNA stability
GO:0061157 mRNA destabilization	IMP PMID:24386402 Effects of the yeast RNA-binding protein Whi3 on the half-li...	ACCEPT	Summary: Cai & Futcher: CLN3 mRNA half-life and the abundance of hundreds of GCAU-rich mRNAs increase in whi3 cells. Reason: Direct mRNA decay measurements (GAL shut-off) plus genome-wide abundance; core biological role of Whi3 binding. Supporting Evidence: PMID:24386402 the whi3 mutation causes a small but consistent increase in the abundance of hundreds of mRNAs, including the CLN3 mRNA PMID:24386402 We suggest that Whi3 may be a very broadly-acting, but mild, modulator of mRNA stability
GO:0071554 cell wall organization or biogenesis	IMP PMID:18667435 Whi3, a developmental regulator of budding yeast, binds a la...	KEEP AS NON CORE	Summary: CACAO. Colomina et al.: whi3 and whi3-dRRM cells are Congo red and Calcofluor white sensitive, show a sorbitol-remediable 37 C growth delay, elevated phospho-Slt2, and are synthetic lethal with slt2 (Fig. 4). Reason: CACAO row. Several independent cell-integrity assays (PMC full text, Fig. 4), RRM-dependent, support the term, and Whi3 binds many mRNAs encoding cell wall proteins, giving a plausible mechanism. The evidence is phenotypic and the grouping term 'organization or biogenesis' is appropriately broad. It is an indirect consequence of Whi3's mRNA regulation, so it is kept as non-core rather than accepted as core. Supporting Evidence: PMID:18667435 we have observed that cell wall integrity is compromised in Whi3-deficient cells and found strong genetic interactions between WHI3 and the cell integrity pathway PMID:18667435 Whi3-associated mRNAs are enriched in clusters of the tetranucleotide GCAU, and mutation of the GCAU clusters in the CLN3 mRNA caused a reduction in its association to Whi3
GO:0017148 negative regulation of translation	IMP PMID:24386402 Effects of the yeast RNA-binding protein Whi3 on the half-li...	NEW	Summary: Whi3 represses CLN3 mRNA translation: whi3 increases CLN3 translational efficiency by ribosome profiling, and inactivation of Whi3 by super-assembly frees Cln3 from translational inhibition. Reason: Whi3 itself performs the regulatory step: as an RRM protein bound to 5' GCAU motifs of CLN3 mRNA it lowers its translation (Cai & Futcher ribosome profiling; Caudron & Barral). This is a direct, mechanistic consequence of its binding, not a downstream phenotype, and it is missing from GOA. Supporting Evidence: PMID:24386402 In addition, the whi3 mutation causes a small increase in the translational efficiency of CLN3 mRNA PMID:24315096 This acquired behavior depends on super-assembly and inactivation of the G1/S inhibitor Whi3, which liberates the G1 cyclin Cln3 from translational inhibition

Gene Description

Existing Annotations Review

Core Functions

Sequence-specific binding of GCAU-motif-containing mRNAs (CLN3 and hundreds of membrane, secretory and cell wall protein mRNAs) by the C-terminal RRM in the cytoplasm, promoting their destabilization and, for CLN3, repressing translation.

Dose-dependent inhibitor of Start: by restraining CLN3 mRNA and retaining Cln3-Cdc28 in the cytoplasm (with ER association), Whi3 delays the G1/S transition and sets a larger critical cell size; inactivation by super-assembly (mnemon) after deceptive courtship or in old cells frees Cln3.

References

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