The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The requested protein is correctly identified. In Schizosaccharomyces pombe, srw1 and ste9 refer to the same locus/protein; the principal literature also describes it as a conserved Hct1/Cdh1/Fizzy-related WD-repeat protein. This matches the supplied UniProt accession O13286, ORF SPAC144.13c, organism strain 972/ATCC 24843, and CDC20/Fizzy–WD40 domain assignments. No evidence from similarly named genes in other organisms was used. (kitamura1998fissionyeastste9 pages 1-2, kitamura1998fissionyeastste9 pages 11-12, yamaguchi2000fissionyeastfizzy‐related pages 1-2, kitamura1998fissionyeastste9 pages 2-3)
Srw1/Ste9 is not an enzyme acting alone. It is a regulatory, substrate-selecting coactivator of the anaphase-promoting complex/cyclosome (APC/C), a multisubunit ubiquitin E3 ligase. Its best-established function is to promote APC/C-dependent destruction of the mitotic B-type cyclin Cdc13 during G1, thereby keeping Cdc2/CDK activity low. This enables pre-Start G1 arrest, prevents premature mitosis, and permits mating and differentiation under nitrogen starvation. It also targets the MBF transcriptional activator Rep2, with this activity inhibited by the replication checkpoint during S-phase arrest. (kitamura1998fissionyeastste9 pages 1-2, yamaguchi2000fissionyeastfizzy‐related pages 1-2, kitamura1998fissionyeastste9 pages 11-12, chu2009acds1mediatedcheckpoint pages 1-2, kominami1998apc10andste9srw1 pages 1-2)
Direct Ste9-focused research in 2023–2024 is sparse. Recent studies have expanded the quantitative and stress-regulatory context of the fission-yeast APC/C, but they do not overturn the functional annotation established by the foundational 1997–2009 studies and refined mechanistically in 2020.
| Aspect | Best-supported conclusion | Evidence type / experiment | Confidence / caveat | Key study year and DOI URL |
|---|---|---|---|---|
| Identity and family | Srw1 and Ste9 designate the same Schizosaccharomyces pombe protein, a conserved Hct1/Cdh1/Fizzy-related WD-repeat family member, consistent with UniProt O13286 and its CDC20/Fizzy–WD40 domains. | Gene cloning/complementation, sequence comparison, and independent genetic characterization (kitamura1998fissionyeastste9 pages 1-2, yamaguchi2000fissionyeastfizzy‐related pages 1-2, kitamura1998fissionyeastste9 pages 2-3) | High. Direct organism- and locus-specific evidence; no evidence from similarly named genes in other organisms was used. | 1998: 10.1091/mbc.9.5.1065; 2000: 10.1093/emboj/19.15.3968 |
| Primary biochemical role | Srw1/Ste9 is a substrate-selecting APC/C coactivator and regulatory adapter, not an enzyme that independently catalyzes a reaction. Its WD-repeat platform is inferred to recruit destruction-motif-bearing substrates to the APC/C ubiquitin ligase. | Genetic and cell-biological evidence links Ste9 to APC/C-dependent proteolysis; conserved Cdh1/Fizzy-family architecture supports the adapter mechanism (yamaguchi2000fissionyeastfizzy‐related pages 1-2, kitamura1998fissionyeastste9 pages 11-12, kominami1998apc10andste9srw1 pages 1-2) | High for APC/C coactivation; moderate for the precise structural recognition mechanism in Srw1 itself. Early studies proposed recruitment before Ste9-specific structural or fully reconstituted biochemical evidence was available. | 1998: 10.1093/emboj/17.18.5388; 2000: 10.1093/emboj/19.15.3968 |
| Cdc13/cyclin-B substrate | APC/C–Srw1/Ste9 promotes G1-specific destruction of the mitotic B-type cyclin Cdc13, thereby lowering Cdc2–Cdc13 kinase activity. It is required for Cdc13 turnover during G1 arrest but not for the distinct destruction pathway operating at mitotic exit. | Cdc13 persists in G1-arrested ste9 mutants; Ste9 overexpression lowers Cdc13 and histone-H1 kinase activity and can permit genome rereplication; phosphatase-sensitive Srw1 forms correlate with regulation (kitamura1998fissionyeastste9 pages 1-2, kitamura1998fissionyeastste9 pages 11-12, yamaguchi2000fissionyeastfizzy‐related pages 1-2) | High for functional targeting and degradation control. The cited evidence is stronger than a mere family-based inference, although early studies did not fully reconstitute Cdc13 ubiquitylation with purified Ste9. | 1998: 10.1091/mbc.9.5.1065; 2000: 10.1093/emboj/19.15.3968 |
| Rep2 substrate and replication checkpoint | The MBF transcriptional activator Rep2 is an APC/C–Ste9 proteolytic target. During hydroxyurea-induced S-phase arrest, Rad3–Cds1 checkpoint signaling phosphorylates/inhibits Ste9, stabilizing Rep2 and sustaining MBF-dependent replication and recovery genes. | Cell-cycle protein measurements and ubiquitination/APC/C-dependence tests; Cds1 phosphorylated Ste9 in vitro, and Ste9 inhibition/phosphorylation during S-phase arrest depended on Cds1 (chu2009acds1mediatedcheckpoint pages 1-2) | High for checkpoint-dependent Rep2 protection and APC/C–Ste9 involvement. The exact molecular consequence of every Ste9 phosphorylation site is less completely resolved. | 2009: 10.1128/MCB.00562-09 |
| Phosphorylation and PP2A-B56/Par1 | Ste9 activity is controlled by phosphorylation state: CDK-associated phosphorylation inhibits its G1 function, whereas PP2A-B56/Par1 is required for efficient Ste9 dephosphorylation and APC/C–Ste9 activation during pre-Start G1. | Phosphatase treatment collapsed slower-migrating Srw1 species; nitrogen-starvation time courses showed defective Ste9 dephosphorylation and impaired Cdc13 degradation in par1Δ cells (yamaguchi2000fissionyeastfizzy‐related pages 1-2, stonyte2020requirementofpp2ab56par1 pages 13-14) | High for phosphorylation and Par1 dependence; moderate for direct dephosphorylation. No canonical B56-binding motif was identified, so Par1 may act indirectly by changing CDK activity or through another factor. | 2000: 10.1093/emboj/19.15.3968; 2020: 10.1016/j.isci.2020.101063 |
| Nitrogen-starvation G1 arrest | Ste9 cooperates with the CDK inhibitor Rum1 to establish low CDK activity during nutrient deprivation. Whereas wild-type cells generally divide twice and arrest in G1 after nitrogen withdrawal, ste9/srw1-pathway mutants can complete an additional S phase and arrest with G2 DNA content. | Mutant screens, flow cytometry, cell-cycle-arrest assays, and Cdc13 measurements during nitrogen starvation (kitamura1998fissionyeastste9 pages 1-2, stonyte2020requirementofpp2ab56par1 pages 13-14, kominami1998apc10andste9srw1 pages 1-2) | High. Reproduced by independent genetic studies and mechanistically connected to defective Cdc13 removal. | 1998: 10.1091/mbc.9.5.1065; 1998: 10.1093/emboj/17.18.5388; 2020: 10.1016/j.isci.2020.101063 |
| Differentiation and sterility | ste9/srw1 mutants are sterile or mating-defective primarily because they fail to enter or maintain the pre-Start G1 state required for conjugation and differentiation; suppression by cig2 mutation supports excessive cyclin-CDK activity as an important cause. | Loss-of-function phenotypes, nitrogen-starvation assays, mating analysis, and genetic suppression by cig2 (kitamura1998fissionyeastste9 pages 1-2, kitamura1998fissionyeastste9 pages 11-12, kominami1998apc10andste9srw1 pages 1-2) | High for sterility and its association with failed G1 arrest; moderate for all downstream differentiation mechanisms. Ste9 is important but not generally essential for vegetative viability. | 1998: 10.1091/mbc.9.5.1065; 1998: 10.1093/emboj/17.18.5388 |
| Cellular localization | The available retrieved primary evidence does not establish a precise, dynamically validated subcellular localization for endogenous Srw1/Ste9. Its established substrates and APC/C role place its critical action in the intracellular cell-cycle machinery, with a likely nuclear component, but this is inference rather than direct localization evidence. | No decisive endogenous live-cell imaging or localization experiment was recovered in the Ste9-specific evidence set (kitamura1998fissionyeastste9 pages 1-2, kitamura1998fissionyeastste9 pages 11-12, chu2009acds1mediatedcheckpoint pages 1-2) | Low/uncertain for a specific compartment. It would be inappropriate to assign an exclusive nuclear, cytoplasmic, spindle-pole, or other localization from the cited studies alone. | Evidence gap in the principal 1998–2020 studies; representative foundation: 10.1091/mbc.9.5.1065 |
| 2023–2024 research status | No retrieved 2023–2024 study substantially revises the direct functional annotation of Srw1/Ste9. Recent work instead expands APC/C pathway context, including quantitative meiotic proteome/phosphoproteome resources and stress-dependent control of the alternative APC/C coactivator Slp1/Cdc20. These findings should not be misattributed to Ste9. | A 2024 meiotic survey quantified 4,673 proteins and 7,172 phosphosites, with 2,680 protein levels and 4,005 phosphosites changing significantly; 2024 mechanistic studies examined Pmk1-dependent Slp1 regulation, not Srw1/Ste9 (sun2024negativeregulationof pages 9-10, sun2024negativeregulationof pages 19-21, sun2024negativeregulationof pages 7-8, sivakova2024quantitativeproteomicsand pages 20-21) | High regarding literature scope. These are relevant resources and pathway developments, but only indirect context for O13286; the latest retrieved Ste9-focused mechanistic study is from 2020. | 2024: 10.1038/s41598-024-74523-0; 2024: 10.7554/eLife.97896 |
Table: Evidence matrix distinguishing experimentally supported functions of fission-yeast Srw1/Ste9 from structural inference and broader APC/C pathway context. It also highlights unresolved localization and the scarcity of direct 2023–2024 Ste9 research.
The 1998 Ste9 study cloned the S. pombe locus by complementation and identified Ste9 as homologous to budding-yeast Hct1/Cdh1 and metazoan Fizzy-related proteins. The same study connects ste9 with srw1, while the 2000 study explicitly calls the product the “fission yeast Fizzy-related protein srw1p.” Cdh1/Fizzy-related proteins contain a conserved C-terminal WD-repeat region; this agrees with the supplied InterPro annotations for Cdc20/Fizzy and WD40-repeat domains. (kitamura1998fissionyeastste9 pages 1-2, yamaguchi2000fissionyeastfizzy‐related pages 1-2, kitamura1998fissionyeastste9 pages 2-3)
The WD40 architecture is functionally appropriate for an APC/C coactivator: it provides a protein-interaction platform rather than a catalytic active site. Accordingly, Srw1/Ste9 should be annotated as a cell-cycle regulatory adapter and APC/C substrate receptor/coactivator, not as an autonomous ubiquitin ligase, enzyme, transporter, or structural cytoskeletal protein. The catalytic ubiquitin-transfer machinery resides in the APC/C and its associated E2 enzymes; Ste9 confers activation and substrate-selection properties.
The APC/C is an E3 ubiquitin ligase that polyubiquitylates selected cell-cycle regulators for proteasomal destruction. Srw1/Ste9 is the fission-yeast Cdh1-like coactivator that is most active in late mitosis/G1 and during G1 arrest. Its WD-repeat domain is expected, by family conservation, to participate in recognition of degradation motifs in substrates and their presentation to APC/C. The precise atomic substrate-recognition mechanism has not been solved specifically for O13286 in the retrieved literature, so this structural description is partly homolog-based inference.
Early Ste9 experiments were genetic and cell biological rather than purified-component biochemical reconstitutions. Nevertheless, several convergent observations establish the proteolysis model: Cdc13 persists in G1-arrested ste9 mutants; Ste9 overexpression lowers Cdc13 abundance and Cdc2–Cdc13/H1-histone kinase activity; and excess Ste9 can permit an additional round of DNA replication. The original investigators therefore concluded that Ste9 controls mitotic cyclin abundance through proteolysis. (kitamura1998fissionyeastste9 pages 1-2, kitamura1998fissionyeastste9 pages 11-12)
The best-established physiological substrate is Cdc13, the major mitotic B-type cyclin. Srw1/Ste9 is required for G1-specific Cdc13 destruction but is not required for the separate wave of Cdc13 degradation at mitotic exit. Thus, fission yeast employs at least two temporally distinguishable cyclin-B destruction regimes: Slp1/Cdc20-dependent activity around anaphase and Srw1/Ste9-dependent maintenance of low Cdc13 during G1. (yamaguchi2000fissionyeastfizzy‐related pages 1-2)
This distinction explains the primary phenotype. Without Ste9, residual or accumulating Cdc13 sustains Cdc2 kinase activity when cells should be in pre-Start G1. Conversely, Ste9 overproduction lowers mitotic CDK activity sufficiently to inhibit mitosis and support genome rereplication. The effect is regulatory rather than a direct catalytic reaction by Srw1 itself. (kitamura1998fissionyeastste9 pages 1-2, kitamura1998fissionyeastste9 pages 11-12)
Cig2, an S-phase cyclin, has also been implicated genetically because cig2 mutation partially suppresses ste9 sterility. This supports excessive cyclin-CDK activity as a cause of the phenotype, but the retrieved evidence is weaker for Cig2 as a direct APC/C–Ste9 substrate than it is for Cdc13. (kitamura1998fissionyeastste9 pages 1-2, kitamura1998fissionyeastste9 pages 11-12)
Rep2, an activating component of the MBF G1/S transcription factor, is another experimentally supported APC/C–Ste9 target. Rep2 levels oscillate, peak in G1 with MBF activity, and are controlled through ubiquitin-mediated proteolysis requiring APC/C function. During hydroxyurea-induced replication arrest, the Rad3–Cds1 checkpoint protects Rep2 by inhibiting Ste9: Cds1 phosphorylated Ste9 in vitro, and Ste9 phosphorylation/inhibition during arrest depended on Cds1. Stabilized Rep2 sustains MBF-dependent expression of genes needed for DNA replication, nucleotide production, S-phase regulation, and recovery. (chu2009acds1mediatedcheckpoint pages 1-2)
This mechanism gives Ste9 a precise checkpoint role: under an unperturbed G1 program, APC/C–Ste9 limits Rep2; under replication stress, Cds1 restrains Ste9 so that Rep2 and the S-phase transcriptional response remain active. This is more specific than describing Ste9 simply as a pleiotropic cell-cycle inhibitor.
Ams2 has been reported elsewhere as an APC/C-dependent G1 proteolysis target associated with coupling histone-gene expression to DNA replication, but the full primary text was not available in the retrieved evidence set. It should therefore be considered a literature-supported candidate rather than assigned the same evidence weight here as Cdc13 or Rep2.
Slp1/Cdc20 is an alternative APC/C coactivator and can itself undergo APC/C-associated turnover. However, the retrieved 2024 Slp1 studies investigated Pmk1-dependent phosphorylation and degradation of Slp1, not direct regulation of Srw1/Ste9. Those results must not be misattributed to O13286. (sun2024negativeregulationof pages 9-10, sun2024negativeregulationof pages 19-21, sun2024negativeregulationof pages 7-8)
Srw1 appeared as multiple electrophoretic species in proliferating cells; phosphatase treatment removed the slower-migrating forms, directly demonstrating phosphorylation. The functional model is a reciprocal switch: Cdc2–Cdc13 phosphorylation inhibits Srw1/Ste9 during proliferative cell-cycle stages, whereas dephosphorylation activates it in G1. Active APC/C–Ste9 then degrades Cdc13, further reducing CDK activity and reinforcing G1. (yamaguchi2000fissionyeastfizzy‐related pages 1-2)
This creates a bistable regulatory relationship:
Rum1, the G1 CDK inhibitor, acts alongside Ste9. Rum1 directly inhibits CDK complexes, while Ste9 removes mitotic cyclin. Their partially overlapping activities establish and maintain the low-CDK state needed before Start. ste9 rum1 double mutants remain viable, indicating redundancy and network robustness rather than absolute Ste9 essentiality. (kitamura1998fissionyeastste9 pages 11-12)
A 2020 study identified PP2A-B56^Par1 as necessary for robust Ste9 activation during pre-Start G1. In nitrogen-starvation time courses extending to 300 minutes, par1Δ impaired Ste9 dephosphorylation and Cdc13 degradation and compromised proper G1 arrest. Experiments with inducible phosphorylation-resistant Rum1 further separated Par1 effects on Rum1 stability from effects on Ste9 activation. (stonyte2020requirementofpp2ab56par1 pages 13-14)
The safest mechanistic interpretation is that PP2A-B56^Par1 is required for Ste9 dephosphorylation, not necessarily that Ste9 is a proven direct Par1 substrate. No canonical B56-binding motif was identified in Ste9; Par1 could act through a noncanonical interaction, another phosphatase component, or indirectly by lowering CDK activity. (stonyte2020requirementofpp2ab56par1 pages 13-14)
The Cds1 pathway reverses the normal G1 logic under stalled replication. Cds1-mediated Ste9 phosphorylation inhibits APC/C–Ste9 and prevents Rep2 destruction, maintaining the transcriptional program needed to survive and recover from replication arrest. Thus, distinct kinases regulate Ste9 in different contexts: cyclin-CDK activity restrains it during normal cycle progression, whereas Cds1 restrains it during replication stress to preserve Rep2. (chu2009acds1mediatedcheckpoint pages 1-2)
Wild-type fission yeast responds to nitrogen removal by undergoing approximately two divisions and arresting in G1. ste9/srw1-pathway mutants fail to establish this arrest correctly; they can execute an additional S phase and accumulate with G2 DNA content. The phenotype is shared with defects in Apc10 and Rum1, demonstrating that APC/C-dependent proteolysis and direct CDK inhibition cooperate to enforce nutrient-responsive G1 arrest. (kitamura1998fissionyeastste9 pages 1-2, kominami1998apc10andste9srw1 pages 1-2)
The biochemical explanation is coherent: failure to eliminate Cdc13 leaves excessive CDK activity, causing cells to pass Start rather than remain in mating-competent pre-Start G1. The 2020 Par1 study linked this phenotype to defective Ste9 dephosphorylation and impaired Cdc13 destruction. (stonyte2020requirementofpp2ab56par1 pages 13-14)
ste9 mutants are sterile or strongly mating-defective under nitrogen starvation. This is principally an indirect consequence of failing to enter the appropriate pre-Start G1 differentiation state, rather than evidence that Ste9 is a dedicated transcription factor for mating genes. Partial suppression by cig2 mutation supports inappropriate cyclin-CDK activity as an important causal mechanism. (kitamura1998fissionyeastste9 pages 1-2, kitamura1998fissionyeastste9 pages 11-12, kominami1998apc10andste9srw1 pages 1-2)
Ste9 is therefore important for coupling environmental nutrient information to cell-cycle exit and sexual differentiation. It is not generally essential for vegetative growth, although it becomes critical in sensitized backgrounds; for example, genetic interactions with wee1 reveal that Ste9-mediated cyclin removal is especially important when inhibitory control of Cdc2 is compromised. (kitamura1998fissionyeastste9 pages 1-2, kitamura1998fissionyeastste9 pages 11-12)
Overexpressing Ste9 decreases Cdc13–Cdc2 activity and can induce an extra DNA-replication round, whereas ste9 mutation suppresses rereplication caused by Cdc2 inactivation. These findings place Ste9 upstream of replication competence through removal of mitotic CDK activity. Ste9 is not a replication enzyme; it resets the CDK state that permits replication origins to become competent. (kitamura1998fissionyeastste9 pages 11-12)
The retrieved Ste9-specific primary literature does not provide sufficiently strong endogenous imaging evidence to assign O13286 an exclusive compartment. Its established interaction with APC/C and its effects on Cdc13, Rep2, and nuclear cell-cycle transitions imply an important intracellular and likely nuclear functional pool, but “nuclear localization” should be treated as a mechanistic inference rather than a directly established exclusive localization.
Accordingly, the conservative annotation is: intracellular APC/C-associated cell-cycle regulator, acting on substrates that control nuclear cell-cycle events; precise dynamic localization unresolved in the retrieved evidence. There is no basis here to call it secreted, membrane-bound, extracellular, or organelle-specific.
No retrieved 2023–2024 publication directly revises the molecular annotation of Srw1/Ste9. The most recent focused mechanistic paper recovered was the 2020 PP2A-B56^Par1 study. This scarcity should not be interpreted as uncertainty about the core function; rather, Ste9’s classification as the fission-yeast Cdh1-type APC/C coactivator is mature, and recent work has concentrated on broader APC/C regulation and systems-level resources.
A 2024 S. pombe meiotic proteomics/phosphoproteomics study quantified 4,673 proteins and 7,172 phosphosites. It reported significant meiotic changes in 2,680 protein levels and 4,005 phosphorylation sites, providing a large resource in which APC/C regulators and their phosphorylation dynamics can be investigated. The study cites Ste9-related work but does not itself establish a new Ste9 mechanism. Publication: October 2024, DOI 10.1038/s41598-024-74523-0. (sivakova2024quantitativeproteomicsand pages 20-21)
Two 2024 studies addressed stress regulation of the alternative APC/C activator Slp1/Cdc20. Pmk1 binds Slp1 through N-terminal docking sequences, phosphorylates Thr480, and promotes APC/C/Apc15-associated Slp1 turnover; key nearby ubiquitylation residues include Lys472 and Lys479. These findings demonstrate how environmental stress is integrated with APC/C activation in fission yeast, but they concern Slp1, not Srw1/Ste9. Publication: October 2024, DOI 10.7554/eLife.97896. (sun2024negativeregulationof pages 9-10, sun2024negativeregulationof pages 19-21, sun2024negativeregulationof pages 7-8)
Srw1/Ste9 is principally a basic-research and systems-biology tool, not a current clinical target. Its applications include:
Translation to mammals must remain explicitly homolog-based: human CDH1/FZR1 is analogous, but observations in S. pombe Ste9 are not automatically evidence for a human disease mechanism or therapeutic intervention.
Recommended primary annotation:
Srw1/Ste9 is the Cdh1/Fizzy-related WD40 coactivator of the S. pombe anaphase-promoting complex/cyclosome. It promotes ubiquitin-dependent proteolysis of Cdc13/cyclin B during G1, maintaining low Cdc2 activity required for pre-Start G1 arrest, replication competence, and nutrient-induced sexual differentiation. Its activity is inhibited by phosphorylation and promoted during G1 by dephosphorylation requiring PP2A-B56^Par1. During replication arrest, Cds1-dependent inhibition of APC/C–Ste9 stabilizes the MBF activator Rep2 and sustains the S-phase transcriptional response.
Evidence confidence: high for identity, family assignment, G1 Cdc13 control, nitrogen-starvation arrest, and Rep2 checkpoint regulation; moderate for direct molecular details of substrate-motif recognition and direct Par1–Ste9 dephosphorylation; low or unresolved for a precise exclusive subcellular localization.
References
(kitamura1998fissionyeastste9 pages 1-2): Kenji Kitamura, Hiromi Maekawa, and Chikashi Shimoda. Fission yeast ste9, a homolog of hct1/cdh1 and fizzy-related, is a novel negative regulator of cell cycle progression during g1-phase. Molecular biology of the cell, 9 5:1065-80, May 1998. URL: https://doi.org/10.1091/mbc.9.5.1065, doi:10.1091/mbc.9.5.1065. This article has 139 citations and is from a domain leading peer-reviewed journal.
(kitamura1998fissionyeastste9 pages 11-12): Kenji Kitamura, Hiromi Maekawa, and Chikashi Shimoda. Fission yeast ste9, a homolog of hct1/cdh1 and fizzy-related, is a novel negative regulator of cell cycle progression during g1-phase. Molecular biology of the cell, 9 5:1065-80, May 1998. URL: https://doi.org/10.1091/mbc.9.5.1065, doi:10.1091/mbc.9.5.1065. This article has 139 citations and is from a domain leading peer-reviewed journal.
(yamaguchi2000fissionyeastfizzy‐related pages 1-2): Satoko Yamaguchi, Hiroto Okayama, and Paul Nurse. Fission yeast fizzy‐related protein srw1p is a g1‐specific promoter of mitotic cyclin b degradation. The EMBO Journal, 19:3968-3977, Aug 2000. URL: https://doi.org/10.1093/emboj/19.15.3968, doi:10.1093/emboj/19.15.3968. This article has 87 citations.
(kitamura1998fissionyeastste9 pages 2-3): Kenji Kitamura, Hiromi Maekawa, and Chikashi Shimoda. Fission yeast ste9, a homolog of hct1/cdh1 and fizzy-related, is a novel negative regulator of cell cycle progression during g1-phase. Molecular biology of the cell, 9 5:1065-80, May 1998. URL: https://doi.org/10.1091/mbc.9.5.1065, doi:10.1091/mbc.9.5.1065. This article has 139 citations and is from a domain leading peer-reviewed journal.
(chu2009acds1mediatedcheckpoint pages 1-2): Zhaoqing Chu, Majid Eshaghi, Suk Yean Poon, and Jianhua Liu. A cds1-mediated checkpoint protects the mbf activator rep2 from ubiquitination by anaphase-promoting complex/cyclosome-ste9 at s-phase arrest in fission yeast. Sep 2009. URL: https://doi.org/10.1128/mcb.00562-09, doi:10.1128/mcb.00562-09. This article has 17 citations and is from a domain leading peer-reviewed journal.
(kominami1998apc10andste9srw1 pages 1-2): Kin-ichiro Kominami, Helena Seth-Smith, and Takashi Toda. Apc10 and ste9/srw1, two regulators of the apc–cyclosome, as well as the cdk inhibitor rum1 are required for g1 cell‐cycle arrest in fission yeast. The EMBO Journal, 17:5388-5399, Sep 1998. URL: https://doi.org/10.1093/emboj/17.18.5388, doi:10.1093/emboj/17.18.5388. This article has 123 citations.
(stonyte2020requirementofpp2ab56par1 pages 13-14): Vilte Stonyte, Ruth Martín, Dario Segura-Peña, Nikolina Sekulić, and Sandra Lopez-Aviles. Requirement of pp2a-b56par1 for the stabilization of the cdk inhibitor rum1 and activation of apc/cste9 during pre-start g1 in s. pombe. iScience, 23:101063, May 2020. URL: https://doi.org/10.1016/j.isci.2020.101063, doi:10.1016/j.isci.2020.101063. This article has 8 citations and is from a peer-reviewed journal.
(sun2024negativeregulationof pages 9-10): Li Sun, Xuejin Chen, Chunlin Song, Wenjing Shi, Libo Liu, Shuang Bai, Xi Wang, Jiali Chen, Chengyu Jiang, Shuang-min Wang, Zhou-qing Luo, Ruiwen Wang, Yamei Wang, and Quan-wen Jin. Negative regulation of apc/c activation by mapk-mediated attenuation of cdc20slp1 under stress. Oct 2024. URL: https://doi.org/10.7554/elife.97896, doi:10.7554/elife.97896. This article has 4 citations and is from a domain leading peer-reviewed journal.
(sun2024negativeregulationof pages 19-21): Li Sun, Xuejin Chen, Chunlin Song, Wenjing Shi, Libo Liu, Shuang Bai, Xi Wang, Jiali Chen, Chengyu Jiang, Shuang-min Wang, Zhou-qing Luo, Ruiwen Wang, Yamei Wang, and Quan-wen Jin. Negative regulation of apc/c activation by mapk-mediated attenuation of cdc20slp1 under stress. Oct 2024. URL: https://doi.org/10.7554/elife.97896, doi:10.7554/elife.97896. This article has 4 citations and is from a domain leading peer-reviewed journal.
(sun2024negativeregulationof pages 7-8): Li Sun, Xuejin Chen, Chunlin Song, Wenjing Shi, Libo Liu, Shuang Bai, Xi Wang, Jiali Chen, Chengyu Jiang, Shuang-min Wang, Zhou-qing Luo, Ruiwen Wang, Yamei Wang, and Quan-wen Jin. Negative regulation of apc/c activation by mapk-mediated attenuation of cdc20slp1 under stress. Oct 2024. URL: https://doi.org/10.7554/elife.97896, doi:10.7554/elife.97896. This article has 4 citations and is from a domain leading peer-reviewed journal.
(sivakova2024quantitativeproteomicsand pages 20-21): Barbara Sivakova, Anja Wagner, Miroslava Kretova, Jana Jakubikova, Juraj Gregan, Klaus Kratochwill, Peter Barath, and Lubos Cipak. Quantitative proteomics and phosphoproteomics profiling of meiotic divisions in the fission yeast schizosaccharomyces pombe. Scientific Reports, Oct 2024. URL: https://doi.org/10.1038/s41598-024-74523-0, doi:10.1038/s41598-024-74523-0. This article has 11 citations and is from a peer-reviewed journal.