or
Title | Rkp1/CPC2, a RACK1 homolog, interacts with Pck1 to regulate PKC-mediated signaling in Schizosaccharomyces pombe |
Authors | Mi Sun Won; Young Joo Jang; Kwang Lae Hoe; J Y Park; Kyung Sook Chung; Dong Uk Kim; N K Sun; S A Kim; K B Song; Hyang Sook Yoo |
Publisher | The Korean Society for Applied Microbiology |
Issue Date | 2002 |
Citation | Journal of Microbiology and Biotechnology, vol. 12, no. 4, pp. 592-597 |
Keywords | CPC2; Pck1; RACK1; Rkp1; schizosaccharomyces pombe; activated protein C; calcium; guanine nucleotide binding protein; myelin basic protein; protein kinase C |
Abstract | The Rkp1/CPC2, a receptor for activated protein kinase C of Schizosaccharomyces pombe, contains seven WD motifs found in the G-protein β-subunit. A 110-kDa protein was identified to interact with Rkp1/CPC2 by immunoprecipitation and following in vitro binding assay. To examine its kinase activity and binding ability to Rkp1, the pck1+, a PKC homolog of S. pombe, was cloned. Pck1 phosphorylated myelin basic protein (MBP) and histone H1 in a phospholipid-dependent and Ca2+-independent manner. It was demonstrated that the N-terminal region of Pck1 was responsible for the binding to Rkp1, thus suggesting that Rkp1 interacted with Pck1 to regulate Pck1-mediated signaling in S. pombe. |
ISSN | 1017-7825 |
Appears in Collections | |
Registered Date |
2017-04-19 |
