User:Marcin Jozef Suskiewicz/Sandbox Parvin/

From Proteopedia

Alpha-parvin^[1], also known as actopaxin^[2] or CH domain-containing ILK-binding protein (CH-ILK-BP)^[3] is an adapter protein known to interact with a number of focal adhesion proteins leading to focal adhesion stabilisation. Knock-out analysis confirmed it to be essential for efficient directional cell migration during embryogenesis in mice^[4]. Spatially and temporarily regulated dynamic changes in the phosphorylation status of alpha-parvin at serines 4 and 8 and consequent changes in affinities towards its binding partners (icluding CdGAP, TESK1 and possibly others) may be responsible for 1) focal adhesion turnover (disassembly of old adhesions, assembly of new ones) and 2) actin cytoskeleton reorganization, two interrelated processes contributing to cell migration.^[5][6][7][8]