Parvin: Difference between revisions

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{{STRUCTURE_3kmw| PDB=3kmw | SIZE=400| SCENE= |right|CAPTION=Alpha-parvin complex with integrin-linked kinase pseudokinase domain and ATP, [[3kmw]] }}

[[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>

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Revision as of 22:19, 25 July 2011 view source David Canner (talk \| contribs) 7,699 edits No edit summary ← Older edit		Revision as of 10:11, 11 April 2012 view source Michal Harel (talk \| contribs) 32,826 edits No edit summary Newer edit →
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			{{STRUCTURE_3kmw\| PDB=3kmw \| SIZE=400\| SCENE= \|right\|CAPTION=Alpha-parvin complex with integrin-linked kinase pseudokinase domain and ATP, [[3kmw]] }}


	[[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>