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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
21
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pubmed:dateCreated |
1998-6-25
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pubmed:databankReference |
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pubmed:abstractText |
After receiving an external stimulus Dictyostelium amoebae are able to rearrange their actin cytoskeleton within seconds, and phosphorylation is a prime candidate for quick modification of cytoskeletal components. We isolated a kinase from cytosolic extracts that specifically phosphorylated severin, a Ca2+-dependent F-actin fragmenting protein. In gel filtration chromatography severin kinase eluted with a molecular mass of about 300 kDa and contained a 62-kDa component whose autophosphorylation caused a mobility shift in SDS-polyacrylamide gel electrophoresis and stimulated phosphorylation of severin. Severin kinase activity could be specifically precipitated with antibodies raised against the 62-kDa polypeptide. Phosphorylation of severin was strongly reduced in the presence of Ca2+, indicating additional regulation at the substrate level. Peptide sequencing and cloning of the cDNA demonstrated that the 62-kDa protein belongs to the Ste20p- or p21-activated protein kinase family. It is most closely related to the germinal center kinase subfamily with its N-terminal positioned catalytic domain followed by a presumptive regulatory domain at the C terminus. The presence of a Ste20-like severin kinase in Dictyostelium suggests a direct signal transduction from the plasma membrane to the cytoskeleton by phosphorylation of actin-binding proteins.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
22
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pubmed:volume |
273
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12952-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9582328-Amino Acid Sequence,
pubmed-meshheading:9582328-Animals,
pubmed-meshheading:9582328-Chromatography, Gel,
pubmed-meshheading:9582328-Chromatography, Ion Exchange,
pubmed-meshheading:9582328-Cloning, Molecular,
pubmed-meshheading:9582328-Dictyostelium,
pubmed-meshheading:9582328-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:9582328-Evolution, Molecular,
pubmed-meshheading:9582328-Fungal Proteins,
pubmed-meshheading:9582328-Humans,
pubmed-meshheading:9582328-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:9582328-Microfilament Proteins,
pubmed-meshheading:9582328-Molecular Sequence Data,
pubmed-meshheading:9582328-Phosphorylation,
pubmed-meshheading:9582328-Protein-Serine-Threonine Kinases,
pubmed-meshheading:9582328-Protozoan Proteins,
pubmed-meshheading:9582328-Rabbits,
pubmed-meshheading:9582328-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:9582328-Sequence Homology, Amino Acid
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pubmed:year |
1998
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pubmed:articleTitle |
Characterization and cloning of a Dictyostelium Ste20-like protein kinase that phosphorylates the actin-binding protein severin.
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pubmed:affiliation |
Adolf-Butenandt-Institut/Zellbiologie, Ludwig-Maximilians-Universität, Schillerstrasse 42, 80336 München, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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