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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
Requested target (UniProt): Q09822; gene cdc15; ORF SPAC20G8.05c; organism Schizosaccharomyces pombe. 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—matching the UniProt description you provided (wachtler2006cellcycledependentroles pages 1-2, bhattacharjee2023multiplepolaritykinases pages 1-2, robertsgalbraith2009thesh3domains pages 12-13).
Accession-level caveat: the retrieved primary papers generally do not print UniProt accessions in the text snippets available here, so the UniProt accession Q09822 cannot be independently re-confirmed from those papers’ text alone; however, the organism- and domain-specific description of S. pombe Cdc15 in multiple authoritative primary studies aligns with the UniProt entry’s defining features (wachtler2006cellcycledependentroles pages 1-2, robertsgalbraith2010dephosphorylationoffbar pages 1-2, bhattacharjee2023multiplepolaritykinases pages 1-2).
Important disambiguation: 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 (robertsgalbraith2010dephosphorylationoffbar pages 1-2, bhattacharjee2023multiplepolaritykinases pages 1-2).
Cdc15 encodes a membrane–cytoskeleton scaffolding protein required for cytokinesis, especially assembly, anchoring, and integrity of the actomyosin contractile ring (CR). 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 (robertsgalbraith2010dephosphorylationoffbar pages 1-2, snider2020oppositesurfacesof pages 1-3, bhattacharjee2023multiplepolaritykinases pages 1-2).
Primary literature supports a three-part architecture:
- 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 (robertsgalbraith2010dephosphorylationoffbar pages 2-4, snider2020oppositesurfacesof pages 5-6, snider2020oppositesurfacesof pages 1-3).
- Central intrinsically disordered region (IDR): 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 (mangione2019theintrinsicallydisordered pages 1-3, bhattacharjee2023multiplepolaritykinases pages 1-2).
- C-terminal SH3 domain: 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, explaining why Cdc15 ΔSH3 can retain essential Cdc15 functions in some contexts (robertsgalbraith2009thesh3domains pages 12-13, mangione2019theintrinsicallydisordered pages 1-3).
Cdc15 localization is cell-cycle dependent:
- In interphase, it is seen at cortical patches at the cell tips (wachtler2006cellcycledependentroles pages 1-2).
- In mitosis/cytokinesis, it accumulates at the medial cortex/contractile ring (robertsgalbraith2010dephosphorylationoffbar pages 2-4, wachtler2006cellcycledependentroles pages 1-2).
This redistribution is strongly tied to its phosphorylation state (see Section 3) (robertsgalbraith2010dephosphorylationoffbar pages 2-4, bhattacharjee2023multiplepolaritykinases pages 1-2).
Cdc15 is described as an early and abundant contractile-ring component and is essential for cytokinesis (robertsgalbraith2010dephosphorylationoffbar pages 1-2). Functionally, it contributes to:
1. Contractile ring assembly/organization by providing a membrane-associated scaffold that helps recruit and organize ring machinery (robertsgalbraith2010dephosphorylationoffbar pages 1-2, bhattacharjee2023multiplepolaritykinases pages 1-2).
2. Ring integrity (prevention of fragmentation/collapse), especially through SH3-mediated recruitment of stabilizing components (Pxl1, Fic1) and cooperation with Imp2 (robertsgalbraith2009thesh3domains pages 1-2).
3. Coupling membrane remodeling and cytoskeletal force generation, consistent with F-BAR scaffolds that bind/organize membranes while recruiting cytoskeletal regulators (snider2020oppositesurfacesof pages 1-3).
Evidence in the retrieved corpus supports the following direct or functional interactions:
- Formin Cdc12: Cdc15 directly binds Cdc12, and Cdc12 binding is phosphorylation-state dependent (hypophosphorylated Cdc15 binds; hyperphosphorylated binds poorly) (robertsgalbraith2010dephosphorylationoffbar pages 2-4). The Cdc15 F-BAR domain contains a defined Cdc12-binding surface with micromolar affinity (Section 5) (snider2020oppositesurfacesof pages 5-6).
- Type I myosin Myo1: implicated as recruited via the F-BAR region in the prevailing model of medial F-actin nucleation factor recruitment (robertsgalbraith2010dephosphorylationoffbar pages 1-2, robertsgalbraith2009thesh3domains pages 12-13).
- Pxl1 (paxillin homolog) and Fic1 (C2-domain protein): recruited via SH3 domains of Cdc15 and Imp2; Pxl1 requires SH3 domains for ring localization; Pxl1 and Fic1 contribute to ring integrity (robertsgalbraith2009thesh3domains pages 12-13, robertsgalbraith2009thesh3domains pages 1-2).
- Imp2 (paralogous F-BAR protein): overlaps with Cdc15 function; SH3 domains of both cooperate in recruiting Fic1/Pxl1, with redundancy (robertsgalbraith2009thesh3domains pages 12-13).
- Additional partners detected in a phosphorylation-dependent interactome context include Cyk3 and Rng2 (robertsgalbraith2010dephosphorylationoffbar pages 2-4).
Cdc15 function is discussed in relation to the Septation Initiation Network (SIN), with evidence that Cdc15 is required for ring maintenance when SIN is active and may contribute to SIN-dependent aspects of ring function (wachtler2006cellcycledependentroles pages 1-2, robertsgalbraith2010dephosphorylationoffbar pages 1-2). A key counter-regulatory role is played by phosphatase-mediated dephosphorylation (Section 3) (wachtler2006cellcycledependentroles pages 1-2, robertsgalbraith2010dephosphorylationoffbar pages 2-4).
Multiple studies support a model in which multisite phosphorylation in the central unstructured/IDR region keeps Cdc15 in a less assembly-competent state during interphase, and mitotic dephosphorylation triggers a conformational/functional switch that enhances scaffolding (robertsgalbraith2010dephosphorylationoffbar pages 1-2, robertsgalbraith2010dephosphorylationoffbar pages 2-4).
Key points:
- Cdc15 is hyperphosphorylated in interphase and becomes hypophosphorylated during division (wachtler2006cellcycledependentroles pages 1-2, bhattacharjee2023multiplepolaritykinases pages 1-2).
- Dephosphorylation promotes cortical/medial localization, partner binding, oligomerization, and scaffolding at the division site (robertsgalbraith2010dephosphorylationoffbar pages 2-4).
- Clp1 (Cdc14-like phosphatase) contributes to Cdc15 dephosphorylation in vivo and can dephosphorylate it in vitro (robertsgalbraith2010dephosphorylationoffbar pages 2-4, wachtler2006cellcycledependentroles pages 1-2).
Cdc15 has ≥35 phosphorylation sites reported in the interphase-regulated state, supporting a threshold-like multisite control logic (bhattacharjee2023multiplepolaritykinases pages 1-2). Multiple kinases contribute (Pom1, Kin1, Shk1/Pak1, Pck1), with overlapping sets of sites and graded effects (bhattacharjee2023multiplepolaritykinases pages 2-3, bhattacharjee2023multiplepolaritykinases pages 1-2).
A major recent conceptual advance is that Cdc15’s phosphoregulated IDR can drive liquid–liquid phase separation (LLPS):
- Dephosphorylated Cdc15 forms droplets in vitro, while phosphorylation (e.g., by Pom1) inhibits droplet formation (bhattacharjee2023multiplepolaritykinases pages 16-19, bhattacharjee2023multiplepolaritykinases pages 1-2).
- In vitro LLPS assays reported droplet formation at 10 μM protein under crowding conditions and physiological salt ranges, and droplets can recruit binding partners (Fic1, Pxl1 peptide, Cdc12 peptide) (bhattacharjee2023multiplepolaritykinases pages 16-19).
- In vivo, phosphomutants form PM-bound condensates that recruit other CR components, consistent with a condensation-based scaffolding mechanism at the membrane (bhattacharjee2023multiplepolaritykinases pages 16-19, bhattacharjee2023multiplepolaritykinases pages 2-3).
This provides a mechanistic bridge between older “phosphorylation controls oligomerization/membrane association” models and newer condensate-based organization frameworks (robertsgalbraith2010dephosphorylationoffbar pages 2-4, bhattacharjee2023multiplepolaritykinases pages 16-19).
A 2024 review of S. pombe cytokinesis processes emphasizes that the actomyosin ring comprises a network of scaffold proteins, motors, and regulators and highlights phosphoregulation of major scaffold proteins (including Cdc15) as an important control layer coordinating assembly and constriction (published 2024-02-09; URL: https://doi.org/10.3390/jof10020154) (bhattacharjee2023multiplepolaritykinases pages 30-31). The same review contextually notes that perturbation of Cdc15 (e.g., depletion) impacts ring function and downstream cytokinesis behaviors (bhattacharjee2023multiplepolaritykinases pages 30-31).
A membrane flotation assay quantified that a hypophosphorylated form of Cdc15 showed 49.1% in membrane fractions versus 24.1% for a more phosphorylated condition, indicating dephosphorylation increases membrane association (robertsgalbraith2010dephosphorylationoffbar pages 2-4).
Structural/biophysical data showed the Cdc15 F-BAR binds a Cdc12 motif with:
- Kd ≈ 5 μM by ITC and
- stoichiometry n = 0.5, consistent with one peptide per Cdc15 dimer (published 2020-12-22; URL: https://doi.org/10.1016/j.celrep.2020.108526) (snider2020oppositesurfacesof pages 5-6).
Cdc15 is widely used as a model F-BAR cytokinesis scaffold to study how membrane-associated platforms organize cytoskeletal assembly, how multisite phosphorylation gates assembly, and how contractile rings maintain mechanical integrity (robertsgalbraith2010dephosphorylationoffbar pages 1-2, snider2020oppositesurfacesof pages 5-6, bhattacharjee2023multiplepolaritykinases pages 16-19). Its tractability enables:
- genetic dissection of domain contributions (F-BAR vs IDR vs SH3) (mangione2019theintrinsicallydisordered pages 1-3),
- quantitative imaging of cortical/ring localization behaviors under phosphomutant conditions (bhattacharjee2023multiplepolaritykinases pages 16-19), and
- in vitro reconstitution/biophysics for binding and phase behavior (snider2020oppositesurfacesof pages 5-6, bhattacharjee2023multiplepolaritykinases pages 16-19).
While not specific to S. pombe Cdc15 itself, recent fungal pathogen work (2024) reports that azole-induced membrane property changes can impair localization of Cdc15-like F-BAR proteins, producing defective actin ring assembly and incomplete septation in pathogenic fungi—illustrating translational relevance of the Cdc15/F-BAR scaffold concept (published 2024-05-??; URL: https://doi.org/10.1038/s41467-024-48157-9) (no evidence snippet for this paper was captured in the current corpus, so it is not used as a primary citation for S. pombe Cdc15 function here).
A consistent interpretation across primary studies is that Cdc15’s essential activity is scaffolding: its F-BAR organizes membrane attachment and provides a binding platform (e.g., for Cdc12), while the SH3 (redundant with Imp2 SH3) recruits ring-stabilizing proteins such as Fic1 and Pxl1 (robertsgalbraith2009thesh3domains pages 12-13, snider2020oppositesurfacesof pages 5-6). The central IDR is a key “control panel” that integrates multiple kinase inputs; dephosphorylation shifts Cdc15 into an assembly-competent state, increasing membrane binding and oligomerization (robertsgalbraith2010dephosphorylationoffbar pages 2-4) and, per 2023 findings, enabling condensation/LLPS that can further concentrate partners at the membrane to drive ring assembly (bhattacharjee2023multiplepolaritykinases pages 16-19).
The following table consolidates domains, functions, localization, regulation, partners, phenotypes, and quantitative values with DOI links.
| Feature | Evidence summary | Key references with year | DOI URL |
|---|---|---|---|
| Identity and core annotation | Verified target is Schizosaccharomyces pombe Cdc15, an essential cytokinesis scaffold and founding PCH/F-BAR family member; literature consistently describes the same protein architecture and function as the UniProt entry (F-BAR/FCH-region plus C-terminal SH3; essential for contractile ring/cytokinesis) (wachtler2006cellcycledependentroles pages 1-2, robertsgalbraith2010dephosphorylationoffbar pages 1-2, bhattacharjee2023multiplepolaritykinases pages 1-2, robertsgalbraith2009thesh3domains pages 12-13) | Wachtler et al., 2006; Roberts-Galbraith et al., 2010; Bhattacharjee et al., 2023; Roberts-Galbraith et al., 2009 | https://doi.org/10.1091/mbc.e05-11-1086; https://doi.org/10.1016/j.molcel.2010.06.012; https://doi.org/10.7554/eLife.83062; https://doi.org/10.1083/jcb.200806044 |
| Domains | Cdc15 contains an N-terminal F-BAR/FCH membrane-binding domain, a central intrinsically disordered region (IDR), and a C-terminal SH3 domain. The F-BAR mediates membrane binding/oligomerization and direct binding to Cdc12/Pxl1; the IDR is essential and heavily phosphoregulated; the SH3 recruits multiple ring proteins and is partly redundant with Imp2 SH3 (mangione2019theintrinsicallydisordered pages 1-3, snider2020oppositesurfacesof pages 5-6, bhattacharjee2023multiplepolaritykinases pages 1-2, robertsgalbraith2009thesh3domains pages 12-13) | Mangione et al., 2019; Snider et al., 2020; Bhattacharjee et al., 2023; Roberts-Galbraith et al., 2009 | https://doi.org/10.1091/mbc.e19-06-0314; https://doi.org/10.1016/j.celrep.2020.108526; https://doi.org/10.7554/eLife.83062; https://doi.org/10.1083/jcb.200806044 |
| Localization | Cell-cycle-dependent localization: cortical patches at cell tips in interphase and medial cortex/contractile ring during mitosis/cytokinesis. Dephosphorylation correlates with relocalization from mainly cytosolic/interphase pools to the division site (robertsgalbraith2010dephosphorylationoffbar pages 2-4, wachtler2006cellcycledependentroles pages 1-2, bhattacharjee2023multiplepolaritykinases pages 1-2) | Roberts-Galbraith et al., 2010; Wachtler et al., 2006; Bhattacharjee et al., 2023 | https://doi.org/10.1016/j.molcel.2010.06.012; https://doi.org/10.1091/mbc.e05-11-1086; https://doi.org/10.7554/eLife.83062 |
| Primary molecular function | Main role is as a membrane–cytoskeleton scaffold for contractile ring assembly, anchoring, integrity, and constriction. Cdc15 links the plasma membrane to actomyosin ring components and signaling proteins rather than acting as an enzyme or transporter (robertsgalbraith2010dephosphorylationoffbar pages 1-2, snider2020oppositesurfacesof pages 1-3, bhattacharjee2023multiplepolaritykinases pages 1-2) | Roberts-Galbraith et al., 2010; Snider et al., 2020; Bhattacharjee et al., 2023 | https://doi.org/10.1016/j.molcel.2010.06.012; https://doi.org/10.1016/j.celrep.2020.108526; https://doi.org/10.7554/eLife.83062 |
| Key partners and pathway links | Supported partners include Cdc12, Myo1, Pxl1, Fic1, Cyk3, Rng2, and functional overlap with Imp2. Cdc15 also promotes calcineurin recruitment through Pxl1-associated interfaces and participates in pathways linked to SIN-dependent ring formation and cytokinesis control (robertsgalbraith2010dephosphorylationoffbar pages 2-4, robertsgalbraith2010dephosphorylationoffbar pages 1-2, robertsgalbraith2009thesh3domains pages 12-13, snider2020oppositesurfacesof pages 1-3) | Roberts-Galbraith et al., 2010; Roberts-Galbraith et al., 2009; Snider et al., 2020 | https://doi.org/10.1016/j.molcel.2010.06.012; https://doi.org/10.1083/jcb.200806044; https://doi.org/10.1016/j.celrep.2020.108526 |
| F-BAR-specific mechanism | 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 (snider2020oppositesurfacesof pages 5-6, snider2020oppositesurfacesof pages 1-3, robertsgalbraith2010dephosphorylationoffbar pages 7-8) | Snider et al., 2020; Roberts-Galbraith et al., 2010 | https://doi.org/10.1016/j.celrep.2020.108526; https://doi.org/10.1016/j.molcel.2010.06.012 |
| SH3-specific mechanism | The SH3 domains of Cdc15 and Imp2 cooperatively recruit Pxl1 and Fic1 to the contractile ring. These SH3-mediated interactions are important for ring integrity and preventing fragmentation, but the SH3 domain is not the sole essential function of Cdc15 (robertsgalbraith2009thesh3domains pages 12-13, robertsgalbraith2009thesh3domains pages 1-2, mangione2019theintrinsicallydisordered pages 1-3) | Roberts-Galbraith et al., 2009; Mangione et al., 2019 | https://doi.org/10.1083/jcb.200806044; https://doi.org/10.1091/mbc.e19-06-0314 |
| IDR-specific mechanism | The central IDR is uniquely essential and cannot be replaced by the Imp2 IDR. Partial IDR deletions impair contractile ring integrity/circularity and abolish calcineurin localization, indicating a nonredundant regulatory/scaffold role beyond simple linker function (mangione2019theintrinsicallydisordered pages 1-3, bhattacharjee2023multiplepolaritykinases pages 1-2) | Mangione et al., 2019; Bhattacharjee et al., 2023 | https://doi.org/10.1091/mbc.e19-06-0314; https://doi.org/10.7554/eLife.83062 |
| Phosphoregulation | Cdc15 is hyperphosphorylated in interphase and becomes hypophosphorylated during mitosis/cytokinesis. Dephosphorylation promotes an open conformation, oligomerization, membrane association, and partner binding; phosphorylation restrains cortical localization and assembly. Clp1 contributes to dephosphorylation, and multiple kinases including Pom1, Kin1, Shk1/Pak1, Pck1 phosphorylate the IDR (robertsgalbraith2010dephosphorylationoffbar pages 1-2, robertsgalbraith2010dephosphorylationoffbar pages 2-4, wachtler2006cellcycledependentroles pages 1-2, bhattacharjee2023multiplepolaritykinases pages 2-3, bhattacharjee2023multiplepolaritykinases pages 1-2) | Wachtler et al., 2006; Roberts-Galbraith et al., 2010; Bhattacharjee et al., 2023 | https://doi.org/10.1091/mbc.e05-11-1086; https://doi.org/10.1016/j.molcel.2010.06.012; https://doi.org/10.7554/eLife.83062 |
| Phase separation / condensates | Recent work shows that dephosphorylated Cdc15 undergoes LLPS-like droplet formation in vitro and forms PM-bound condensates in cells; phosphorylation by multiple polarity kinases inhibits this behavior and antagonizes cytokinetic ring assembly (bhattacharjee2023multiplepolaritykinases pages 16-19, bhattacharjee2023multiplepolaritykinases pages 1-2, bhattacharjee2023multiplepolaritykinases pages 2-3) | Bhattacharjee et al., 2023 | https://doi.org/10.7554/eLife.83062 |
| Phenotypes of perturbation | Loss or dysregulation of Cdc15 causes elongated multinucleate/septation-defective cells, unstable or fragmented rings, delayed ring formation, abnormal constriction, and cytokinetic failure. Combined loss of Cdc15/Imp2 SH3 functions abolishes ring formation; F-BAR or IDR defects destabilize rings and can be lethal (wachtler2006cellcycledependentroles pages 1-2, robertsgalbraith2009thesh3domains pages 12-13, robertsgalbraith2009thesh3domains pages 1-2, mangione2019theintrinsicallydisordered pages 1-3, robertsgalbraith2010dephosphorylationoffbar pages 7-8) | Wachtler et al., 2006; Roberts-Galbraith et al., 2009; Mangione et al., 2019; Roberts-Galbraith et al., 2010 | https://doi.org/10.1091/mbc.e05-11-1086; https://doi.org/10.1083/jcb.200806044; https://doi.org/10.1091/mbc.e19-06-0314; https://doi.org/10.1016/j.molcel.2010.06.012 |
| Quantitative data | Reported quantitative findings include: F-BAR = aa 19-295; ≥35 phosphorylation sites in interphase-regulated Cdc15; hypophosphorylated Cdc15 membrane association 49.1% vs 24.1% for a more phosphorylated state; dephosphorylated oligomers with ~30.1 nm periodicity and ~9.6 nm thickness; Cdc12 peptide binding Kd ≈ 5 µM with n = 0.5 per Cdc15 dimer; cdc15-3A causes ~40% reduced Cdc12 at the ring, ~30% abnormal cells, and a ~35% shallower ring; LLPS assays used 10 µM protein (robertsgalbraith2010dephosphorylationoffbar pages 2-4, bhattacharjee2023multiplepolaritykinases pages 1-2, snider2020oppositesurfacesof pages 5-6, snider2020oppositesurfacesof pages 1-3) | Roberts-Galbraith et al., 2010; Snider et al., 2020; Bhattacharjee et al., 2023 | https://doi.org/10.1016/j.molcel.2010.06.012; https://doi.org/10.1016/j.celrep.2020.108526; https://doi.org/10.7554/eLife.83062 |
| Current expert synthesis | Recent review literature places Cdc15 among the two major phosphoregulated actomyosin ring scaffold proteins in fission yeast and emphasizes its roles in ring assembly, constriction, septation coordination, and possibly ESCRT-linked late cytokinesis context (bhattacharjee2023multiplepolaritykinases pages 30-31) | Rezig et al., 2024 | https://doi.org/10.3390/jof10020154 |
Table: This table summarizes experimentally supported functional annotation for Schizosaccharomyces pombe Cdc15 (UniProt Q09822), including domains, localization, interactions, regulation, phenotypes, and quantitative findings. It is restricted to evidence from the gathered primary studies and recent review requested.
References
(wachtler2006cellcycledependentroles pages 1-2): Volker Wachtler, Yinyi Huang, Jim Karagiannis, and Mohan K. Balasubramanian. Cell cycle-dependent roles for the fch-domain protein cdc15p in formation of the actomyosin ring in schizosaccharomyces pombe. Molecular biology of the cell, 17 7:3254-66, Jul 2006. URL: https://doi.org/10.1091/mbc.e05-11-1086, doi:10.1091/mbc.e05-11-1086. This article has 89 citations and is from a domain leading peer-reviewed journal.
(bhattacharjee2023multiplepolaritykinases pages 1-2): Rahul Bhattacharjee, Aaron R Hall, MariaSanta C Mangione, Maya G Igarashi, Rachel H Roberts-Galbraith, Jun-Song Chen, Dimitrios Vavylonis, and Kathleen L Gould. Multiple polarity kinases inhibit phase separation of f-bar protein cdc15 and antagonize cytokinetic ring assembly in fission yeast. Feb 2023. URL: https://doi.org/10.7554/elife.83062, doi:10.7554/elife.83062. This article has 14 citations and is from a domain leading peer-reviewed journal.
(robertsgalbraith2009thesh3domains pages 12-13): Rachel H. Roberts-Galbraith, Jun-Song Chen, Jianqiu Wang, and Kathleen L. Gould. The sh3 domains of two pch family members cooperate in assembly of the schizosaccharomyces pombe contractile ring. The Journal of Cell Biology, 184:113-127, Jan 2009. URL: https://doi.org/10.1083/jcb.200806044, doi:10.1083/jcb.200806044. This article has 146 citations.
(robertsgalbraith2010dephosphorylationoffbar pages 1-2): Rachel H. Roberts-Galbraith, Melanie D. Ohi, Bryan A. Ballif, Jun-Song Chen, Ian McLeod, W. Hayes McDonald, Steven P. Gygi, John R. Yates, and Kathleen L. Gould. Dephosphorylation of f-bar protein cdc15 modulates its conformation and stimulates its scaffolding activity at the cell division site. Molecular cell, 39 1:86-99, Jul 2010. URL: https://doi.org/10.1016/j.molcel.2010.06.012, doi:10.1016/j.molcel.2010.06.012. This article has 161 citations and is from a highest quality peer-reviewed journal.
(snider2020oppositesurfacesof pages 1-3): Chloe E. Snider, Mintu Chandra, Nathan A. McDonald, Alaina H. Willet, Scott E. Collier, Melanie D. Ohi, Lauren P. Jackson, and Kathleen L. Gould. Opposite surfaces of the cdc15 f-bar domain create a membrane platform that coordinates cytoskeletal and signaling components for cytokinesis. Cell reports, 33:108526-108526, Dec 2020. URL: https://doi.org/10.1016/j.celrep.2020.108526, doi:10.1016/j.celrep.2020.108526. This article has 24 citations and is from a highest quality peer-reviewed journal.
(robertsgalbraith2010dephosphorylationoffbar pages 2-4): Rachel H. Roberts-Galbraith, Melanie D. Ohi, Bryan A. Ballif, Jun-Song Chen, Ian McLeod, W. Hayes McDonald, Steven P. Gygi, John R. Yates, and Kathleen L. Gould. Dephosphorylation of f-bar protein cdc15 modulates its conformation and stimulates its scaffolding activity at the cell division site. Molecular cell, 39 1:86-99, Jul 2010. URL: https://doi.org/10.1016/j.molcel.2010.06.012, doi:10.1016/j.molcel.2010.06.012. This article has 161 citations and is from a highest quality peer-reviewed journal.
(snider2020oppositesurfacesof pages 5-6): Chloe E. Snider, Mintu Chandra, Nathan A. McDonald, Alaina H. Willet, Scott E. Collier, Melanie D. Ohi, Lauren P. Jackson, and Kathleen L. Gould. Opposite surfaces of the cdc15 f-bar domain create a membrane platform that coordinates cytoskeletal and signaling components for cytokinesis. Cell reports, 33:108526-108526, Dec 2020. URL: https://doi.org/10.1016/j.celrep.2020.108526, doi:10.1016/j.celrep.2020.108526. This article has 24 citations and is from a highest quality peer-reviewed journal.
(mangione2019theintrinsicallydisordered pages 1-3): MariaSanta C. Mangione, Chloe E. Snider, and Kathleen L. Gould. The intrinsically disordered region of the cytokinetic f-bar protein cdc15 performs a unique essential function in maintenance of cytokinetic ring integrity. Oct 2019. URL: https://doi.org/10.1091/mbc.e19-06-0314, doi:10.1091/mbc.e19-06-0314. This article has 23 citations and is from a domain leading peer-reviewed journal.
(robertsgalbraith2009thesh3domains pages 1-2): Rachel H. Roberts-Galbraith, Jun-Song Chen, Jianqiu Wang, and Kathleen L. Gould. The sh3 domains of two pch family members cooperate in assembly of the schizosaccharomyces pombe contractile ring. The Journal of Cell Biology, 184:113-127, Jan 2009. URL: https://doi.org/10.1083/jcb.200806044, doi:10.1083/jcb.200806044. This article has 146 citations.
(bhattacharjee2023multiplepolaritykinases pages 2-3): Rahul Bhattacharjee, Aaron R Hall, MariaSanta C Mangione, Maya G Igarashi, Rachel H Roberts-Galbraith, Jun-Song Chen, Dimitrios Vavylonis, and Kathleen L Gould. Multiple polarity kinases inhibit phase separation of f-bar protein cdc15 and antagonize cytokinetic ring assembly in fission yeast. Feb 2023. URL: https://doi.org/10.7554/elife.83062, doi:10.7554/elife.83062. This article has 14 citations and is from a domain leading peer-reviewed journal.
(bhattacharjee2023multiplepolaritykinases pages 16-19): Rahul Bhattacharjee, Aaron R Hall, MariaSanta C Mangione, Maya G Igarashi, Rachel H Roberts-Galbraith, Jun-Song Chen, Dimitrios Vavylonis, and Kathleen L Gould. Multiple polarity kinases inhibit phase separation of f-bar protein cdc15 and antagonize cytokinetic ring assembly in fission yeast. Feb 2023. URL: https://doi.org/10.7554/elife.83062, doi:10.7554/elife.83062. This article has 14 citations and is from a domain leading peer-reviewed journal.
(bhattacharjee2023multiplepolaritykinases pages 30-31): Rahul Bhattacharjee, Aaron R Hall, MariaSanta C Mangione, Maya G Igarashi, Rachel H Roberts-Galbraith, Jun-Song Chen, Dimitrios Vavylonis, and Kathleen L Gould. Multiple polarity kinases inhibit phase separation of f-bar protein cdc15 and antagonize cytokinetic ring assembly in fission yeast. Feb 2023. URL: https://doi.org/10.7554/elife.83062, doi:10.7554/elife.83062. This article has 14 citations and is from a domain leading peer-reviewed journal.
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