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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2002-2-8
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pubmed:databankReference |
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pubmed:abstractText |
The ADF (actin-depolymerizing factor)/cofilin family is a stimulus-responsive mediator of actin dynamics. In contrast to the mechanisms of inactivation of ADF/cofilin by kinases such as LIM-kinase 1 (LIMK1), much less is known about its reactivation through dephosphorylation. Here we report Slingshot (SSH), a family of phosphatases that have the property of F actin binding. In Drosophila, loss of ssh function dramatically increased levels of both F actin and phospho-cofilin (P cofilin) and disorganized epidermal cell morphogenesis. In mammalian cells, human SSH homologs (hSSHs) suppressed LIMK1-induced actin reorganization. Furthermore, SSH and the hSSHs dephosphorylated P cofilin in cultured cells and in cell-free assays. Our results strongly suggest that the SSH family plays a pivotal role in actin dynamics by reactivating ADF/cofilin in vivo.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actin Depolymerizing Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/DSTN protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Destrin,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Homeodomain Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/LHX1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/LIM-Homeodomain Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Monoester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Zyx102EF protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/Zyxin,
http://linkedlifedata.com/resource/pubmed/chemical/ssh protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/testis-specific protein kinase 1
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
108
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
233-46
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:11832213-Actin Depolymerizing Factors,
pubmed-meshheading:11832213-Actins,
pubmed-meshheading:11832213-Amino Acid Sequence,
pubmed-meshheading:11832213-Animals,
pubmed-meshheading:11832213-Cell Line,
pubmed-meshheading:11832213-Cell-Free System,
pubmed-meshheading:11832213-Destrin,
pubmed-meshheading:11832213-Drosophila,
pubmed-meshheading:11832213-Drosophila Proteins,
pubmed-meshheading:11832213-Embryonic Structures,
pubmed-meshheading:11832213-Homeodomain Proteins,
pubmed-meshheading:11832213-Humans,
pubmed-meshheading:11832213-Immunohistochemistry,
pubmed-meshheading:11832213-LIM-Homeodomain Proteins,
pubmed-meshheading:11832213-Microfilament Proteins,
pubmed-meshheading:11832213-Molecular Sequence Data,
pubmed-meshheading:11832213-Phosphoprotein Phosphatases,
pubmed-meshheading:11832213-Phosphoric Monoester Hydrolases,
pubmed-meshheading:11832213-Phosphorylation,
pubmed-meshheading:11832213-Protein Binding,
pubmed-meshheading:11832213-Protein-Serine-Threonine Kinases,
pubmed-meshheading:11832213-Sequence Alignment,
pubmed-meshheading:11832213-Transcription Factors,
pubmed-meshheading:11832213-Zyxin
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pubmed:year |
2002
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pubmed:articleTitle |
Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin.
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pubmed:affiliation |
Department of Molecular Genetics, The Institute for Virus Research, Kyoto University, Kyoto 606-8507, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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