title: Pleckstrin homology domain interacts with Rkp1/Cpc2, a RACK1 homolog, to modulate Pck2-mediated signaling process in Schizosaccharomyces pombe.
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.
authors.affiliation: Genome Research Center, Korea Research Institute of Biotechnology and Bioscience, Taejon, 305-600, Korea. misun@mail.kribb.re.kr
authors.forename: M
authors.initials: M
authors.lastname: Won
authors.forename: Y J
authors.initials: YJ
authors.lastname: Jang
authors.forename: K S
authors.initials: KS
authors.lastname: Chung
authors.forename: D U
authors.initials: DU
authors.lastname: Kim
authors.forename: K L
authors.initials: KL
authors.lastname: Hoe
authors.forename: M Y
authors.initials: MY
authors.lastname: Han
authors.forename: H B
authors.initials: HB
authors.lastname: Kim
authors.forename: S H
authors.initials: SH
authors.lastname: Lee
authors.forename: H W
authors.initials: HW
authors.lastname: Oh
authors.forename: H S
authors.initials: HS
authors.lastname: Yoo
mesh_terms: D001665:Binding Sites; D001798:Blood Proteins / Q000737:chemistry / Q000378:metabolism*; D019204:GTP-Binding Proteins; D006801:Humans; D066298:In Vitro Techniques; D007527:Isoenzymes / Q000737:chemistry / Q000378:metabolism; D009363:Neoplasm Proteins / Q000378:metabolism*; D051966:Phospholipase C gamma; D010750:Phosphoproteins / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D011493:Protein Kinase C / Q000378:metabolism; D017434:Protein Structure, Tertiary; D000075370:Receptors for Activated C Kinase; D011956:Receptors, Cell Surface / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000378:metabolism; D012568:Schizosaccharomyces / Q000378:metabolism*; D029702:Schizosaccharomyces pombe Proteins; D015398:Signal Transduction; D010738:Type C Phospholipases / Q000737:chemistry / Q000378:metabolism
chemical_list: D001798:Blood Proteins; D007527:Isoenzymes; D009363:Neoplasm Proteins; D010750:Phosphoproteins; C419368:RACK1 protein, human; D000075370:Receptors for Activated C Kinase; D011956:Receptors, Cell Surface; D011993:Recombinant Fusion Proteins; D029702:Schizosaccharomyces pombe Proteins; C000617313:cpc2 protein, S pombe; C039077:platelet protein P47; D011493:Protein Kinase C; D010738:Type C Phospholipases; D051966:Phospholipase C gamma; D019204:GTP-Binding Proteins