User:Marcin Jozef Suskiewicz/Sandbox Parvin/

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[[Alpha-parvin]]<ref>PMID: PMID: 11171322</ref>, also known as actopaxin<ref>PMID: 11134073</ref> or CH domain-containing 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. It is crucial for essential directional cell migration during embryogenesis in mice<ref>PMID: 19798050</ref>. Dynamic changes in its phosphorylation status at serines 4 and 8 and consequent changes in affinities towards its binding partners may be responsible for focal adhesion turnover (disassembly of old adhesions, assembly of new ones) observed during cell migration.<ref>PMID: 15353548</ref><ref>PMID: 15353548</ref><ref>PMID: 15817463</ref><ref>PMID: 16860736</ref>
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[[Alpha-parvin]]<ref>PMID: PMID: 11171322</ref>, also known as actopaxin<ref>PMID: 11134073</ref> or CH domain-containing 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>. 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 focal adhesion turnover (disassembly of old adhesions, assembly of new ones) and actin cytoskeleton reorganization observed during cell migration.<ref>PMID: 15353548</ref><ref>PMID: 15353548</ref><ref>PMID: 15817463</ref><ref>PMID: 16860736</ref>

Revision as of 12:51, 6 December 2010

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]. 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 focal adhesion turnover (disassembly of old adhesions, assembly of new ones) and actin cytoskeleton reorganization observed during cell migration.[5][6][7][8]

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Marcin Jozef Suskiewicz

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