Parvins

Parvins are a family of actin-binding adaptor proteins that function as components of focal adhesions in animal cells. The vertebrate parvin family includes alpha-parvin (PARVA), beta-parvin (PARVB), and gamma-parvin (PARVG). They are widely expressed and localize to regions of cell-ECM contact, where they participate in linking integrin receptors to the actin cytoskeleton.

Biochemical role: Parvins typically interact with ILK (integrin-linked kinase) and PINCH as part of the ILK-PINCH-Parvin complex, coordinating signal transduction and structural linkage at adhesion sites. They are involved in regulation of actin dynamics, cell spreading, migration, and adhesion turnover.

Genetics and evolution: The three paralogs arose by gene duplication in vertebrates; homologs are found in other vertebrates and some invertebrates. The proteins share sequence similarity and conserved interaction motifs that mediate their binding partners.

Biological significance and disease: Functional studies in cell lines and animal models show that parvins contribute to proper adhesion and cytoskeletal organization. Disrupted parvin expression or function can affect cell migration and wound healing; aberrant expression patterns have been observed in certain cancers, suggesting potential roles in metastasis.

See also: focal adhesion, ILK, PINCH, cell adhesion, cytoskeleton.