CMS: An adapter molecule involved in cytoskeletal rearrangements
Open accessAbstract
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 NH 2 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.
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CD2AP is involved in cell-cell adhesion, regulates the actin cytoskeleton, and physically interacts with p130CAS (CASS1).
“CD2AP is involved in cell–cell adhesion, regulates the actin cytoskeleton and physically interacts with p130CAS (CASS1) [61, 74].”
From The new genetic landscape of Alzheimer’s disease: from amyloid cascade to genetically driven synaptic failure hypothesis? (2019) · cites this paper as [74]
The Discussion (page unavailable) reports direct binding between human CMS and p130Cas, while the Results and opening summary describe altered actin organization in CMS-expressing cells. The Discussion identifies CD2AP as a mouse homologue of CMS and reports its binding to the adhesion molecule CD2, but this paper does not directly demonstrate CD2AP–p130Cas binding or a role for CD2AP in cell–cell adhesion. (LLM, conf=0.84)
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- Authors
- Kirsch, K. H., Georgescu, M.-M., Ishimaru, S., & Hanafusa, H.
- Affiliations
- Rockefeller University (US)
- Laboratory of Molecular Oncology, The Rockefeller University, 1230 York Avenue, New York, NY 10021
- ORCID
- Kirsch, Kathrin H.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1999-05-25
- Volume
- 96
- Issue
- 11
- Pages
- 6211-6216
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC26861
- OpenAlex
- W2124504624
- Cited by
- 162
- References
- 1
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 2 · 2022: 3 · 2021: 7 · 2020: 2 · 2019: 1 · 2018: 6 · 2017: 7 · 2016: 8 · 2015: 5 · 2014: 7 · 2013: 5 · 2012: 4
- FWCI
- 4.23
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Medical Research Council Canada
- National Institutes of Health
- Medical Research Council
- National Cancer Institute (CA 44356, R35CA044356)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Keywords
- CMS, p130Cas, SH3 domain, actin cytoskeleton remodeling, proline-rich sequences, Src family kinases, Grb2, phosphatidylinositol 3-kinase, actin binding, coiled-coil domain, cell motility, ruffles, leading edge
- MeSH terms
- Adult, Amino Acid Sequence, Animals, Carrier Proteins, Cell Line, Cell Membrane, Cytoskeletal Proteins, Cytoskeleton, Female, Fetus, Humans, Molecular Sequence Data, Organ Specificity, Phosphoproteins, Phosphorylation, Protein-Tyrosine Kinases, Proteins, Recombinant Proteins, Transcription, Genetic, Transfection, Signal Transduction, Gene Library, Retinoblastoma Protein, Sequence Alignment, Sequence Homology, Amino Acid, COS Cells, Phosphatidylinositol 3-Kinases, Adaptor Proteins, Signal Transducing, Retinoblastoma-Like Protein p130, Crk-Associated Substrate Protein
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