Pleckstrin homology domain interacts with Rkp1/Cpc2, a RACK1 homolog, to modulate Pck2-mediated signaling process in Schizosaccharomyces pombe

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Title
Pleckstrin homology domain interacts with Rkp1/Cpc2, a RACK1 homolog, to modulate Pck2-mediated signaling process in Schizosaccharomyces pombe
Author(s)
Mi Sun Won; Young Joo Jang; Kyung Sook ChungDong Uk Kim; Kwang Lae Hoe; Mi Young Han; Hyung Bae Kim; Sang Hee Lee; Hyun Wha Oh; Hyang Sook Yoo
Bibliographic Citation
Biochemical and Biophysical Research Communications, vol. 289, no. 5, pp. 987-992
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-γ1 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.
Keyword
Fission yeastPleckstrin homology domainRACK1Rkp1/Cpc2
ISSN
0006-291X
Publisher
Elsevier
DOI
http://dx.doi.org/10.1006/bbrc.2001.6094
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
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