title: The Cdc15 and Imp2 SH3 domains cooperatively scaffold a network of proteins that redundantly ensure efficient cell division in fission yeast.
abstract: Schizosaccharomyces pombe cdc15 homology (PCH) family members participate in numerous biological processes, including cytokinesis, typically by bridging the plasma membrane via their F-BAR domains to the actin cytoskeleton. Two SH3 domain-containing PCH family members, Cdc15 and Imp2, play critical roles in S. pombe cytokinesis. Although both proteins localize to the contractile ring, with Cdc15 preceding Imp2, only cdc15 is an essential gene. Despite these distinct roles, the SH3 domains of Cdc15 and Imp2 cooperate in the essential process of recruiting other proteins to stabilize the contractile ring. To better understand the connectivity of this SH3 domain-based protein network at the CR and its function, we used a biochemical approach coupled to proteomics to identify additional proteins (Rgf3, Art1, Spa2, and Pos1) that are integrated into this network. Cell biological and genetic analyses of these SH3 partners implicate them in a range of activities that ensure the fidelity of cell division, including promoting cell wall metabolism and influencing cell morphogenesis.
authors.affiliation: Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232.
authors.forename: Liping
authors.initials: L
authors.lastname: Ren
authors.affiliation: Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232.
authors.forename: Alaina H
authors.initials: AH
authors.lastname: Willet
authors.affiliation: Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232.
authors.forename: Rachel H
authors.initials: RH
authors.lastname: Roberts-Galbraith
authors.affiliation: Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232.
authors.forename: Nathan A
authors.initials: NA
authors.lastname: McDonald
authors.affiliation: Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232.
authors.forename: Anna
authors.initials: A
authors.lastname: Feoktistova
authors.affiliation: Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232.
authors.forename: Jun-Song
authors.initials: JS
authors.lastname: Chen
authors.affiliation: Terrence Donnelly Center for Cellular and Biomolecular Research, Banting and Best Department of Medical Research, University of Toronto, Toronto, ON M5G 1L6, Canada.
authors.forename: Haiming
authors.initials: H
authors.lastname: Huang
authors.affiliation: Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232.
authors.forename: Rodrigo
authors.initials: R
authors.lastname: Guillen
authors.affiliation: Terrence Donnelly Center for Cellular and Biomolecular Research, Banting and Best Department of Medical Research, University of Toronto, Toronto, ON M5G 1L6, Canada.
authors.forename: Charles
authors.initials: C
authors.lastname: Boone
authors.affiliation: Terrence Donnelly Center for Cellular and Biomolecular Research, Banting and Best Department of Medical Research, University of Toronto, Toronto, ON M5G 1L6, Canada.
authors.forename: Sachdev S
authors.initials: SS
authors.lastname: Sidhu
authors.affiliation: Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232.
authors.forename: Janel R
authors.initials: JR
authors.lastname: Beckley
authors.affiliation: Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232 kathy.gould@vanderbilt.edu.
authors.forename: Kathleen L
authors.initials: KL
authors.lastname: Gould
mesh_terms: D000595:Amino Acid Sequence; D018797:Cell Cycle Proteins / Q000235:genetics / Q000378:metabolism*; D002455:Cell Division; D048749:Cytokinesis; D003598:Cytoskeletal Proteins / Q000235:genetics / Q000378:metabolism*; D019204:GTP-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D053263:Gene Regulatory Networks; D020662:Guanine Nucleotide Exchange Factors / Q000235:genetics / Q000378:metabolism; D015151:Immunoblotting; D008164:Luminescent Proteins / Q000235:genetics / Q000378:metabolism; D018613:Microscopy, Confocal; D008969:Molecular Sequence Data; D009154:Mutation; D011485:Protein Binding; D020543:Proteome / Q000235:genetics / Q000378:metabolism; D040901:Proteomics / Q000379:methods; D012568:Schizosaccharomyces / Q000235:genetics / Q000378:metabolism*; D029702:Schizosaccharomyces pombe Proteins / Q000235:genetics / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D059008:Time-Lapse Imaging / Q000379:methods; D018909:src Homology Domains
chemical_list: C082279:CDC15 protein; D018797:Cell Cycle Proteins; D003598:Cytoskeletal Proteins; D020662:Guanine Nucleotide Exchange Factors; C535064:IMP2 protein, S pombe; D008164:Luminescent Proteins; D020543:Proteome; C502214:Rgf3 protein, S pombe; D029702:Schizosaccharomyces pombe Proteins; D019204:GTP-Binding Proteins