Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 63, Issue 1, Pages 25-35Publisher
SPRINGER BASEL AG
DOI: 10.1007/s00018-005-5355-1
Keywords
parvin; ILK; PINCH; paxillin; alpha-actinin; actin cytoskeleton; cell migration; survival
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Funding
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [K08HL068714] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [R01DK054639] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM065188] Funding Source: NIH RePORTER
- NHLBI NIH HHS [HL068714] Funding Source: Medline
- NIDDK NIH HHS [DK54639] Funding Source: Medline
- NIGMS NIH HHS [GM65188] Funding Source: Medline
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The parvins are a family of proteins involved in linking integrins and associated proteins with intracellular pathways that regulate actin cytoskeletal dynamics and cell survival. Both alpha-parvin (PARVA) and beta-parvin (PARVB) localize to focal adhesions and function in cell adhesion, spreading, motility and survival through interactions with partners, such as integrin-linked kinase (ILK), paxillin, alpha-actinin and testicular kinase 1. A complex of PARVA with ILK and the LIM protein PINCH-1 is critical for cell survival in a variety of cells, including certain cancer cells, kidney podocytes and cardiac myocytes. While PARVA inhibits the activities of Rac1 and testicular kinase 1 and cell spreading, PARVB binds alpha PIX and alpha-actinin, and can promote cell spreading. In contrast to PARVA, PARVB inhibits ILK activity and reverses some of its oncogenic effects in cancer cells. This review focuses on the structure and function of the parvins and some possible roles in human diseases.
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