Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library.
The PCH family protein, Cdc15p, recruits two F-actin nucleation pathways to coordinate cytokinetic actin ring formation in Schizosaccharomyces pombe.
Spatial and temporal pathway for assembly and constriction of the contractile ring in fission yeast cytokinesis.
Organization of a sterol-rich membrane domain by cdc15p during cytokinesis in fission yeast.
Etd1p is a novel protein that links the SIN cascade with cytokinesis.
Cell cycle-dependent roles for the FCH-domain protein Cdc15p in formation of the actomyosin ring in Schizosaccharomyces pombe.
ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe.
Assembly of the cytokinetic contractile ring from a broad band of nodes in fission yeast.
The Clp1/Cdc14 phosphatase contributes to the robustness of cytokinesis by association with anillin-related Mid1.
The SH3 domains of two PCH family members cooperate in assembly of the Schizosaccharomyces pombe contractile ring.
A spatial gradient coordinates cell size and mitotic entry in fission yeast.
Assembly and architecture of precursor nodes during fission yeast cytokinesis.
Distinct roles for F-BAR proteins Cdc15p and Bzz1p in actin polymerization at sites of endocytosis in fission yeast.
Cytokinesis-based constraints on polarized cell growth in fission yeast.
Separate roles of IQGAP Rng2p in forming and constricting the Schizosaccharomyces pombe cytokinetic contractile ring.
Cooperation between Rho-GEF Gef2 and its binding partner Nod1 in the regulation of fission yeast cytokinesis.
The formins Cdc12 and For3 cooperate during contractile ring assembly in cytokinesis.
Characterization of the roles of Blt1p in fission yeast cytokinesis.
The Cdc15 and Imp2 SH3 domains cooperatively scaffold a network of proteins that redundantly ensure efficient cell division in fission yeast.
The F-BAR Cdc15 promotes contractile ring formation through the direct recruitment of the formin Cdc12.
A formin-nucleated actin aster concentrates cell wall hydrolases for cell fusion in fission yeast.
Oligomerization but Not Membrane Bending Underlies the Function of Certain F-BAR Proteins in Cell Motility and Cytokinesis.
Phosphoinositide-mediated ring anchoring resists perpendicular forces to promote medial cytokinesis.
Nanoscale architecture of the Schizosaccharomyces pombe contractile ring.
Cdk1-dependent phosphoinhibition of a formin-F-BAR interaction opposes cytokinetic contractile ring formation.
A unique kinesin-like protein, Klp8, is involved in mitosis and cell morphology through microtubule stabilization.
DYRK kinase Pom1 drives F-BAR protein Cdc15 from the membrane to promote medial division.
Opposite Surfaces of the Cdc15 F-BAR Domain Create a Membrane Platform That Coordinates Cytoskeletal and Signaling Components for Cytokinesis.
Fission yeast paxillin contains two Cdc15 binding motifs for robust recruitment to the cytokinetic ring.
The S. pombe cdc15 gene is a key element in the reorganization of F-actin at mitosis.
imp2, a new component of the actin ring in the fission yeast Schizosaccharomyces pombe.
Falcon deep research report on S. pombe cdc15
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Cdc15 is an essential cytokinetic scaffold with an N-terminal FCH/F-BAR
module and a C-terminal SH3 domain, localizing to cell tips in interphase
and the medial contractile ring during mitosis.
"The *S. pombe* protein studied in the primary cytokinesis literature is consistently named **Cdc15/Cdc15p**, described as an **essential cytokinetic scaffold** with an **N-terminal FCH/F-BAR module and a C-terminal SH3 domain**, localizing to **cell tips in interphase** and the **medial contractile ring during mitosis**"
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The defining molecular role of Cdc15 is to couple the plasma membrane to
contractile-ring components and regulators, organizing proteins needed to
build and stabilize the ring.
"Its defining molecular role is to **couple the plasma membrane to contractile-ring components and regulators**, organizing proteins needed to build and stabilize the ring and coordinate furrow ingression/septation"
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Cdc15 has a three-part architecture: an N-terminal FCH/F-BAR membrane-binding
domain (platform for recruiting factors including formin Cdc12), a central
intrinsically disordered region that is uniquely essential and the major
substrate for multisite phosphorylation, and a C-terminal SH3 domain.
"- **N-terminal FCH/F-BAR domain**: a dimeric/oligomeric membrane-binding module that acts as a platform for recruiting factors (including the formin Cdc12) and physically linking the ring to the plasma membrane"
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The central IDR is uniquely essential and cannot be replaced by the Imp2 IDR;
it is the major substrate for multisite phosphorylation controlling
conformational state and assembly behavior.
"a regulatory and interaction module that is **uniquely essential** in Cdc15 (cannot be replaced by the Imp2 IDR) and is the major substrate for multisite phosphorylation controlling conformational state and assembly behavior"
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The C-terminal SH3 domain recruits ring proteins (notably Fic1 and Pxl1) and
is partly redundant with the SH3 domain of the paralog Imp2.
"a protein–protein interaction module that recruits specific ring proteins (notably Fic1 and Pxl1) and contributes to ring integrity; it is partly **redundant with the SH3 domain of the paralog Imp2**"
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The Cdc15 F-BAR domain binds the formin Cdc12 with a Kd of approximately 5
micromolar (ITC) at a stoichiometry of one peptide per Cdc15 dimer; Cdc12
binding is phosphorylation-state dependent (hypophosphorylated binds well).
"Cdc15 directly binds Cdc12, and Cdc12 binding is phosphorylation-state dependent (hypophosphorylated Cdc15 binds; hyperphosphorylated binds poorly)"
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Cdc15 is hyperphosphorylated in interphase and becomes hypophosphorylated
during division; dephosphorylation (involving the Clp1/Cdc14-like phosphatase)
promotes cortical/medial localization, oligomerization, and membrane binding.
"Cdc15 is **hyperphosphorylated in interphase** and becomes **hypophosphorylated during division**"
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Multiple polarity kinases (Pom1, Kin1, Shk1/Pak1, Pck1) phosphorylate the IDR;
phosphorylation inhibits Cdc15 liquid-liquid phase separation and antagonizes
cytokinetic ring assembly, whereas dephosphorylated Cdc15 forms droplets in
vitro and PM-bound condensates in cells.
"**Dephosphorylated Cdc15 forms droplets in vitro**, while phosphorylation (e.g., by Pom1) inhibits droplet formation"
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The membrane-binding concave F-BAR surface and the opposite protein-binding
surface create a membrane platform; F-BAR oligomerization (not membrane
bending) is important for stable ring architecture.
"The **concave F-BAR surface** binds membranes, while the **opposite surface** binds protein ligands such as **Cdc12** and **Pxl1**, creating a membrane platform that coordinates cytoskeletal and signaling components. F-BAR oligomerization is important for stable ring architecture"
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S. pombe Cdc15 is an F-BAR/SH3 scaffold, NOT a protein kinase, and should not
be confused with budding yeast Cdc15 (a Mitotic Exit Network kinase).
"do not confuse this target with **budding yeast Cdc15**, which is a **protein kinase** in the Mitotic Exit Network (MEN). The *S. pombe* Cdc15 described here is an **F-BAR/SH3 scaffold**, not a kinase"