title: CMS: an adapter molecule involved in cytoskeletal rearrangements.
abstract: Cas ligand with multiple Src homology (SH) 3 domains (CMS) is an ubiquitously expressed signal transduction molecule that interacts with the focal adhesion protein p130(Cas). CMS contains three SH3 in its NH2 terminus and proline-rich sequences in its center region. The latter sequences mediate the binding to the SH3 domains of p130(Cas), Src-family kinases, p85 subunit of phosphatidylinositol 3-kinase, and Grb2. The COOH-terminal region contains putative actin binding sites and a coiled-coil domain that mediates homodimerization of CMS. CMS is a cytoplasmic protein that colocalizes with F-actin and p130(Cas) to membrane ruffles and leading edges of cells. Ectopic expression of CMS in COS-7 cells resulted in alteration in arrangement of the actin cytoskeleton. We observed a diffuse distribution of actin in small dots and less actin fiber formation. Altogether, these features suggest that CMS functions as a scaffolding molecule with a specialized role in regulation of the actin cytoskeleton.
authors.affiliation: Laboratory of Molecular Oncology, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA. kirschk@rockvax.rockfeller.edu
authors.forename: K H
authors.initials: KH
authors.lastname: Kirsch
authors.forename: M M
authors.initials: MM
authors.lastname: Georgescu
authors.forename: S
authors.initials: S
authors.lastname: Ishimaru
authors.forename: H
authors.initials: H
authors.lastname: Hanafusa
mesh_terms: D048868:Adaptor Proteins, Signal Transducing; D000328:Adult; D000595:Amino Acid Sequence; D000818:Animals; D019556:COS Cells; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D002460:Cell Line; D002462:Cell Membrane / Q000502:physiology / Q000648:ultrastructure; D050719:Crk-Associated Substrate Protein; D003598:Cytoskeletal Proteins; D003599:Cytoskeleton / Q000502:physiology* / Q000648:ultrastructure; D005260:Female; D005333:Fetus; D015723:Gene Library; D006801:Humans; D008969:Molecular Sequence Data; D009928:Organ Specificity; D019869:Phosphatidylinositol 3-Kinases / Q000378:metabolism; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D011505:Protein-Tyrosine Kinases / Q000378:metabolism*; D011506:Proteins; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D016160:Retinoblastoma Protein / Q000378:metabolism; D050717:Retinoblastoma-Like Protein p130; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction; D014158:Transcription, Genetic; D014162:Transfection
chemical_list: D048868:Adaptor Proteins, Signal Transducing; C493841:BCAR1 protein, human; C114545:CD2-associated protein; D002352:Carrier Proteins; D050719:Crk-Associated Substrate Protein; D003598:Cytoskeletal Proteins; D010750:Phosphoproteins; D011506:Proteins; D011994:Recombinant Proteins; D016160:Retinoblastoma Protein; D050717:Retinoblastoma-Like Protein p130; D019869:Phosphatidylinositol 3-Kinases; D011505:Protein-Tyrosine Kinases