Paxillin (IPR001904)

Short name: Paxillin

Overlapping homologous superfamilies


Family relationships


Paxillin is a cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion) [PMID: 7534286, PMID: 7525621]. Extensive tyrosine phosphorylation occurs during integrin-mediated cell adhesion, embryonic development, fibroblast transformation and following stimulation of cells by mitogens that operate through the 7TM family of G-protein-coupled receptors [PMID: 7525621]. Paxillin binds in vitro to the focal adhesion protein vinculin, as well as to the SH3 domain of c-Src, and, when tyrosine phosphorylated, to the SH2 domain of v-Crk [PMID: 7525621]. An N-terminal region has been identified that supports the binding of both vinculin and the focal adhesion tyrosine kinase, pp125Fak [PMID: 7525621].

Paxillin is a 68 kDa protein containing multiple domains, including four tandem C-terminal LIM domains (each of which binds 2 zinc ions); an N-terminal proline-rich domain, which contains a consensus SH3 binding site; and three potential Crk-SH2 binding sites [PMID: 7534286]. The predicted structure of paxillin suggests that it is a unique cytoskeletal protein capable of interaction with a variety of intracellular signalling and structural molecules important in growth control and the regulation of cytoskeletal organisation [PMID: 7534286, PMID: 7525621].

GO terms

Biological Process

GO:0007160 cell-matrix adhesion

Molecular Function

No terms assigned in this category.

Cellular Component

GO:0005856 cytoskeleton

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.