Paxillin is a 68 kDa cytoplasmic protein that localizes to discrete sites of cell attachment to the extracellular matrix called focal adhesions. It is a multi-domain adapter protein capable of interacting with several structural and signaling proteins including vinculin, FAK, PYK2, Src and Crk. Phosphorylation of paxillin in response to integrin-mediated cell adhesion and growth factor stimulation regulates some of these interactions. Thus, paxillin functions as a scaffold for the recruitment of molecules into a signal transduction complex that is closely apposed to the plasma membrane. This is likely to facilitate the efficient processing of external stimuli that modulate important cellular events including cell adhesion, cell motility and growth control. Since paxillin interacts with several proteins known to cause cell transformation, the binding sites for these proteins on paxillin represent potential targets for therapeutic agents.
ABSTRACT
PUBLICATION RECORD
- Publication year
2020
- Venue
International Journal of Biochemistry and Cell Biology
- Publication date
2020-02-02
- Fields of study
Biology, Medicine
- Identifiers
- External record
- Source metadata
Semantic Scholar, PubMed
CITATION MAP
EXTRACTION MAP
CLAIMS
- No claims are published for this paper.
CONCEPTS
- No concepts are published for this paper.
REFERENCES
Showing 1-18 of 18 references · Page 1 of 1