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Pleckstrin homology domain interacts with Rkp1/Cpc2, a RACK1 homolog, to modulate Pck2-mediated signaling process in Schizosaccharomyces pombe.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2001 Dec 21; Vol. 289 (5), pp. 987-92. - Publication Year :
- 2001
-
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.
- Subjects :
- Binding Sites
Blood Proteins chemistry
GTP-Binding Proteins
Humans
In Vitro Techniques
Isoenzymes chemistry
Isoenzymes metabolism
Phospholipase C gamma
Phosphoproteins chemistry
Protein Binding
Protein Kinase C metabolism
Protein Structure, Tertiary
Receptors for Activated C Kinase
Recombinant Fusion Proteins chemistry
Recombinant Fusion Proteins metabolism
Schizosaccharomyces pombe Proteins
Signal Transduction
Type C Phospholipases chemistry
Type C Phospholipases metabolism
Blood Proteins metabolism
Neoplasm Proteins metabolism
Phosphoproteins metabolism
Receptors, Cell Surface metabolism
Schizosaccharomyces metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0006-291X
- Volume :
- 289
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 11741288
- Full Text :
- https://doi.org/10.1006/bbrc.2001.6094