Direct stimulation of receptor-controlled phospholipase D1 by phospho-cofilin

The activity state of cofilin, which controls actin dynamics, is driven by a phosphorylation–dephosphorylation cycle. Phosphorylation of cofilin by LIM‐kinases results in its inactivation, a process supported by 14‐3‐3ζ and reversed by dephosphorylation by slingshot phosphatases. Here we report on a...

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Vydáno v:	The EMBO journal Ročník 26; číslo 19; s. 4189 - 4202
Hlavní autoři:	Han, Li, Stope, Matthias B, de Jesús, Maider López, Oude Weernink, Paschal A, Urban, Martina, Wieland, Thomas, Rosskopf, Dieter, Mizuno, Kensaku, Jakobs, Karl H, Schmidt, Martina
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	Chichester, UK John Wiley & Sons, Ltd 03.10.2007 Nature Publishing Group UK Springer Nature B.V Nature Publishing Group
Témata:	14-3-3 14-3-3 Proteins Actins - genetics Actins - metabolism Cell Line Cellular biology cofilin EMBO37 Gene Expression Humans Inactivation Lim Kinases LIM-kinase1 Molecular biology Mutation Nuclear Proteins - genetics Nuclear Proteins - metabolism phospholipase D Phospholipase D - genetics Phospholipase D - metabolism Phosphorylation Protein Binding - physiology Protein Kinases - genetics Protein Kinases - metabolism Protein Processing, Post-Translational - physiology Receptors, Muscarinic - genetics Receptors, Muscarinic - metabolism Signal transduction slingshot phospholipase D slingshot cofilin LIM‐kinase1 14‐3‐3
ISSN:	0261-4189, 1460-2075
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Shrnutí:	The activity state of cofilin, which controls actin dynamics, is driven by a phosphorylation–dephosphorylation cycle. Phosphorylation of cofilin by LIM‐kinases results in its inactivation, a process supported by 14‐3‐3ζ and reversed by dephosphorylation by slingshot phosphatases. Here we report on a novel cellular function for the phosphorylation–dephosphorylation cycle of cofilin. We demonstrate that muscarinic receptor‐mediated stimulation of phospholipase D1 (PLD1) is controlled by LIM‐kinase, slingshot phosphatase as well as 14‐3‐3ζ, and requires phosphorylatable cofilin. Cofilin directly and specifically interacts with PLD1 and upon phosphorylation by LIM‐kinase1, stimulates PLD1 activity, an effect mimicked by phosphorylation‐mimic cofilin mutants. The interaction of cofilin with PLD1 is under receptor control and encompasses a PLD1‐specific fragment (aa 585–712). Expression of this fragment suppresses receptor‐induced cofilin–PLD1 interaction as well as PLD stimulation and actin stress fiber formation. These data indicate that till now designated inactive phospho‐cofilin exhibits an active cellular function, and suggest that phospho‐cofilin by its stimulatory effect on PLD1 may control a large variety of cellular functions.
Bibliografie:	ark:/67375/WNG-NNNFJZBP-D ArticleID:EMBJ7601852 istex:4303565ADA2839BBA419DD306564C8ED68210D2E ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 These authors contributed equally to this work Present address: Department of Infection Control, Chinese Military Institute of Disease Control & Prevention, Beijing 100071, China
ISSN:	0261-4189 1460-2075
DOI:	10.1038/sj.emboj.7601852