Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Rkp1/CPC2, a RACK1 Homolog, Interacts with Pck1 to Regulate PKC-Mediated Signaling in Schizosaccharomyces pombe

  • Won, Mi-Sun (Genome Research Center, Korea Research Institute of Biotechnology & Bioscience(KRIBB)) ;
  • Jang, Young-Joo (Genome Research Center, Korea Research Institute of Biotechnology & Bioscience(KRIBB)) ;
  • Hoe, Kwang-Lae (Genome Research Center, Korea Research Institute of Biotechnology & Bioscience(KRIBB)) ;
  • Park, Jo-Young (Department of Food and Nutrition, Chungnam University) ;
  • Chung, Kyung-Sook (Genome Research Center, Korea Research Institute of Biotechnology & Bioscience(KRIBB)) ;
  • Kim, Dong-Uk (Genome Research Center, Korea Research Institute of Biotechnology & Bioscience(KRIBB)) ;
  • Sun, Nam-Kyu (Department of Food Science & Technology, Chungnam National University) ;
  • Kim, Sung-Ai (Department of Food and Nutrition, Chungnam Nation University) ;
  • Song, Kyung-Bin (Department of Food Science & Technology, Chungnam National University) ;
  • Yoo, Hyang-Sook (Genome Research Center, Korea Research Institute of Biotechnology & Bioscience(KRIBB))
  • Published : 2002.08.01
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Abstract

The Rkp1/CPC2, a receptor for activated protein kinase C of Schizosaccharomyces pombe, contains seven WD motifs found in the G-protein $\beta$-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. Pckl phosphorylated myelin basic protein (MBP) and histone Hl in a phospholipid-dependent and $Ca^{2+}$-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 Pckl to regulate Pckl-mediated signaling in S. pombe.

Keywords

References

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