Abstract
Rkp1/Cpc2, a fission yeast RACK1 homolog, interacts with Pck2, a PKC homolog, and is involved in the regulation of pck2-mediated signaling process. The N-terminal region of split pleckstrin homology domain (nPH) in human PLC-gamma1 bound to Rkp1/Cpc2 concomitantly with Pck2. nPH inhibited kinase activity of GST-Pck2 purified from Schizosaccharomyces pombe in vitro. The lethality induced by pck2(+) overexpression was suppressed by coexpression of either rkp1(+) or nPH domain. This result suggests that Rkp1/Cpc2 interacts with PH domain-containing protein and regulates the Pck2-mediated signaling process in S. pombe.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Binding Sites
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Blood Proteins / chemistry
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Blood Proteins / metabolism*
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GTP-Binding Proteins
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Humans
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In Vitro Techniques
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Isoenzymes / chemistry
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Isoenzymes / metabolism
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Neoplasm Proteins / metabolism*
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Phospholipase C gamma
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Phosphoproteins / chemistry
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Phosphoproteins / metabolism*
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Protein Binding
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Protein Kinase C / metabolism
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Protein Structure, Tertiary
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Receptors for Activated C Kinase
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Receptors, Cell Surface / metabolism*
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / metabolism
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Schizosaccharomyces / metabolism*
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Schizosaccharomyces pombe Proteins
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Signal Transduction
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Type C Phospholipases / chemistry
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Type C Phospholipases / metabolism
Substances
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Blood Proteins
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Isoenzymes
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Neoplasm Proteins
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Phosphoproteins
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RACK1 protein, human
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Receptors for Activated C Kinase
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Receptors, Cell Surface
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Recombinant Fusion Proteins
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Schizosaccharomyces pombe Proteins
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cpc2 protein, S pombe
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platelet protein P47
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Protein Kinase C
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Type C Phospholipases
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Phospholipase C gamma
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GTP-Binding Proteins