Parvin: Difference between revisions

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Marcin Jozef Suskiewicz, Michal Harel, Alexander Berchansky, David Canner, Jaime Prilusky

Revision as of 16:19, 24 April 2013 view source Alexander Berchansky (talk \| contribs) 29,637 edits No edit summary ← Older edit		Revision as of 16:20, 24 April 2013 view source Alexander Berchansky (talk \| contribs) 29,637 edits No edit summary Newer edit →
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	<StructureSection load='2vzc' size='450' side='right' scene='Alpha-parvin/~~Parvin~~/9' caption=''>		<StructureSection load='2vzc' size='450' side='right' scene='Alpha-parvin/Cv/1' caption=''>
	[[Alpha-parvin]]<ref>PMID: 11171322</ref>, also known as '''actopaxin'''<ref>PMID: 11134073</ref> or CH domain-containing integrin-linked kinase (ILK)-binding protein (CH-ILK-BP)<ref>PMID: 11331308</ref> 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<ref>PMID: 19798050</ref>. 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, e.g. ILK) 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.<ref>PMID: 15353548</ref><ref>PMID: 15817463</ref><ref>PMID: 16860736</ref><ref>PMID: 15872073</ref>		[[Alpha-parvin]]<ref>PMID: 11171322</ref>, also known as '''actopaxin'''<ref>PMID: 11134073</ref> or CH domain-containing integrin-linked kinase (ILK)-binding protein (CH-ILK-BP)<ref>PMID: 11331308</ref> 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<ref>PMID: 19798050</ref>. 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, e.g. ILK) 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.<ref>PMID: 15353548</ref><ref>PMID: 15817463</ref><ref>PMID: 16860736</ref><ref>PMID: 15872073</ref>