PMID- 10339567
OWN - NLM
STAT- MEDLINE
DCOM- 19990624
LR  - 20220309
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 96
IP  - 11
DP  - 1999 May 25
TI  - CMS: an adapter molecule involved in cytoskeletal rearrangements.
PG  - 6211-6
AB  - 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.
FAU - Kirsch, K H
AU  - Kirsch KH
AD  - Laboratory of Molecular Oncology, The Rockefeller University, 1230 York Avenue,
      New York, NY 10021, USA. kirschk@rockvax.rockfeller.edu
FAU - Georgescu, M M
AU  - Georgescu MM
FAU - Ishimaru, S
AU  - Ishimaru S
FAU - Hanafusa, H
AU  - Hanafusa H
LA  - eng
SI  - GENBANK/AF146277
GR  - CA44356/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Adaptor Proteins, Signal Transducing)
RN  - 0 (BCAR1 protein, human)
RN  - 0 (CD2-associated protein)
RN  - 0 (Carrier Proteins)
RN  - 0 (Crk-Associated Substrate Protein)
RN  - 0 (Cytoskeletal Proteins)
RN  - 0 (Phosphoproteins)
RN  - 0 (Proteins)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Retinoblastoma Protein)
RN  - 0 (Retinoblastoma-Like Protein p130)
RN  - EC 2.7.1.- (Phosphatidylinositol 3-Kinases)
RN  - EC 2.7.10.1 (Protein-Tyrosine Kinases)
SB  - IM
MH  - Adaptor Proteins, Signal Transducing
MH  - Adult
MH  - Amino Acid Sequence
MH  - Animals
MH  - COS Cells
MH  - Carrier Proteins/chemistry/*genetics/*metabolism
MH  - Cell Line
MH  - Cell Membrane/physiology/ultrastructure
MH  - Crk-Associated Substrate Protein
MH  - *Cytoskeletal Proteins
MH  - Cytoskeleton/*physiology/ultrastructure
MH  - Female
MH  - Fetus
MH  - Gene Library
MH  - Humans
MH  - Molecular Sequence Data
MH  - Organ Specificity
MH  - Phosphatidylinositol 3-Kinases/metabolism
MH  - Phosphoproteins/*metabolism
MH  - Phosphorylation
MH  - Protein-Tyrosine Kinases/*metabolism
MH  - *Proteins
MH  - Recombinant Proteins/chemistry/metabolism
MH  - Retinoblastoma Protein/metabolism
MH  - Retinoblastoma-Like Protein p130
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - Signal Transduction
MH  - *Transcription, Genetic
MH  - Transfection
PMC - PMC26861
EDAT- 1999/05/26 00:00
MHDA- 1999/05/26 00:01
CRDT- 1999/05/26 00:00
PHST- 1999/05/26 00:00 [pubmed]
PHST- 1999/05/26 00:01 [medline]
PHST- 1999/05/26 00:00 [entrez]
AID - 10.1073/pnas.96.11.6211 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1999 May 25;96(11):6211-6. doi:
      10.1073/pnas.96.11.6211.