Rkp1/CPC2, a RACK1 homolog, interacts with Pck1 to regulate PKC-mediated signaling in Schizosaccharomyces pombe

Cited 0 time in scopus
Metadata Downloads
Title
Rkp1/CPC2, a RACK1 homolog, interacts with Pck1 to regulate PKC-mediated signaling in Schizosaccharomyces pombe
Author(s)
Mi Sun Won; Young Joo Jang; Kwang Lae Hoe; J Y Park; Kyung Sook ChungDong Uk Kim; N K Sun; S A Kim; K B Song; Hyang Sook Yoo
Bibliographic Citation
Journal of Microbiology and Biotechnology, vol. 12, no. 4, pp. 592-597
Publication Year
2002
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.
Keyword
CPC2Pck1RACK1Rkp1schizosaccharomyces pombe
ISSN
1017-7825
Publisher
Korea Soc-Assoc-Inst
Type
Article
Appears in Collections:
Division of Biomedical Research > Personalized Genomic Medicine Research Center > 1. Journal Articles
Division of Research on National Challenges > 1. Journal Articles
Division of Biomedical Research > Rare Disease Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.