ArticleCurrent biology : CB2011
SIN-inhibitory phosphatase complex promotes Cdc11p dephosphorylation and propagates SIN asymmetry in fission yeast.
Article in Current biology : CB, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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45 citing papers in PubMed, 66 citations in OpenAlex.
- Biotinylation-dependent near-neighbor analysis for identification of septation regulators inbioRxiv : the preprint server for biology · 2026Article
- Article
- STRIPAK-associated greenbeard proteins DOC1 and DOC2 regulate MAK2 signaling and sexual development in Sordaria macrospora.PLoS biology · 2026Article
- Distinct STRIPAK subunits drive conserved and subunit-specific signaling programs inbioRxiv : the preprint server for biology · 2026Article
- The fungal STRIPAK complex: Cellular conductor orchestrating growth and pathogenicity.PLoS pathogens · 2025Article
- New mutations in the core Schizosaccharomyces pombe spindle pole body scaffold Ppc89 reveal separable functions in regulating cell division.G3 (Bethesda, Md.) · 2025Article
- STRIPAK, a fundamental signaling hub of eukaryotic development.Microbiology and molecular biology reviews : MMBR · 2024Review
- The Greatwall-Endosulfine-PP2A/B55 pathway regulates entry into quiescence by enhancing translation of Elongator-tunable transcripts.Nature communications · 2024Article
- Transient PP2A SIP complex localization to mitotic SPBs for SIN inhibition is mediated solely by the Csc1 FHA domain.Molecular biology of the cell · 2024Article
- MOB-mediated regulation of septation initiation network (SIN) signaling is required for echinocandin-induced hyperseptation inmSphere · 2024Article
- A role for the carbon source of the cell and protein kinase A in regulating the S. pombe septation initiation network.Journal of cell science · 2024Article
- The Greatwall-Endosulfine-PP2A/B55 pathway controls entry into quiescence by promoting translation of Elongator-tuneable transcripts.Research square · 2023Article
- Fission yeast polycystin Pkd2p promotes cell size expansion and antagonizes the Hippo-related SIN pathway.Journal of cell science · 2022Article
- The STRIPAK component SipC is involved in morphology and cell-fate determination in the nematode-trapping fungus Duddingtonia flagrans.Genetics · 2022Article
- Uncoupling of Mitosis and Cytokinesis Upon a Prolonged Arrest in Metaphase Is Influenced by Protein Phosphatases and Mitotic Transcription in Fission Yeast.Frontiers in cell and developmental biology · 2022Article
- Article
- PP2A Functions during Mitosis and Cytokinesis in Yeasts.International journal of molecular sciences · 2019Review
- Asymmetrical localization of Nup107-160 subcomplex components within the nuclear pore complex in fission yeast.PLoS genetics · 2019Article
- Ser/Thr protein phosphatases in fungi: structure, regulation and function.Microbial cell (Graz, Austria) · 2019Review
- Assembly of a heptameric STRIPAK complex is required for coordination of light-dependent multicellular fungal development with secondary metabolism in Aspergillus nidulans.PLoS genetics · 2019Article
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11 authors at 2 institutions in 2 countries.
Funding
Abstract
backgroundCytokinesis in many eukaryotes involves the function of an actomyosin-based contractile ring. In fission yeast, actomyosin ring maturation and stability require a conserved signaling pathway termed the SIN (septation initiation network). The SIN consists of a GTPase (Spg1p) and three protein kinases, all of which localize to the mitotic spindle pole bodies (SPBs). Two of the SIN kinases, Cdc7p and Sid1p, localize asymmetrically to the newly duplicated SPB in late anaphase. How this asymmetry is achieved is not understood, although it is known that their symmetric localization impairs cytokinesis.
resultsHere we characterize a new Forkhead-domain-associated protein, Csc1p, and identify SIN-inhibitory PP2A complex (SIP), which is crucial for the establishment of SIN asymmetry. Csc1p localizes to both SPBs early in mitosis, is lost from the SPB that accumulates Cdc7p, and instead accumulates at the SPB lacking Cdc7p. Csc1p is required for the dephosphorylation of the SIN scaffolding protein Cdc11p and is thereby required for the recruitment of Byr4p, a component of the GTPase-activating subunit for Spg1p, to the SPB.
conclusionsBecause Cdc7p does not bind to GDP-Spg1p, we propose that the SIP-mediated Cdc11p dephosphorylation and the resulting recruitment of Byr4p are among the earliest steps in the establishment of SIN asymmetry.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.