Pleckstrin Homology Domain Interacts with Rkp1/Cpc2, a RACK1 Homolog, to Modulate Pck2-Mediated Signaling Process in Schizosaccharomyces pombe

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-γ1 bound to Rkp1/Cpc2 concomitantly with Pck2. nPH inhibited kinase activit...

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Veröffentlicht in:	Biochemical and biophysical research communications 2001-12, Vol.289 (5), p.987-992
Hauptverfasser:	Won, Misun, Jang, Young-Joo, Chung, Kyung-Sook, Kim, Dong-Uk, Hoe, Kwang-Lae, Han, Mi-Young, Kim, Hyung-Bae, Lee, Sang-Hee, Oh, Hyun-Wha, Yoo, Hyang-Sook
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding Sites Blood Proteins - chemistry Blood Proteins - metabolism fission yeast GTP-Binding Proteins Humans In Vitro Techniques Isoenzymes - chemistry Isoenzymes - metabolism Neoplasm Proteins - metabolism Pck2 protein Phospholipase C gamma Phosphoproteins - chemistry Phosphoproteins - metabolism pleckstrin homology domain Protein Binding Protein Kinase C - metabolism Protein Structure, Tertiary RACK1 Receptors for Activated C Kinase Receptors, Cell Surface - metabolism Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - metabolism Rkp1 protein Rkp1/Cpc2 Schizosaccharomyces - metabolism Schizosaccharomyces pombe Schizosaccharomyces pombe Proteins Signal Transduction Type C Phospholipases - chemistry Type C Phospholipases - metabolism
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