Rkp1/Cpc2, a fission yeast RACK1 homolog, is involved in actin cytoskeleton organization through protein kinase C, Pck2, signaling

Biochem Biophys Res Commun. 2001 Mar 23;282(1):10-5. doi: 10.1006/bbrc.2001.4535.

Abstract

The Rkp1/Cpc2, a fission yeast RACK1 homolog, interacted with Pck2, one of the known PKC homologs, in vivo and in vitro. The rkp1-deletion mutants (Deltarkp1) are elongated and the pck2-deletion mutant (Deltapck2) showed abnormal morphology. The double-deletion mutant (Deltarkp1Deltapck2) showed more aberrant cell shapes and was sensitive to high salt concentration. Both Deltarkp1 and Deltapck2 cells were sensitive to latrunculin B (Lat B) which inhibits actin polymerization. The cells expressing the human RACK1 homolog complemented the latrunculin B sensitivity of Deltarkp1 indicating that human RACK1 is a functional homolog of Rkp1/Cpc2. We propose that Rkp1/Cpc2 may function as a receptor for Pck2 in the regulation of actin cytoskeleton organization during cell wall synthesis and morphogenesis of Schizosaccharomyces pombe.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism*
  • Cytoskeleton / metabolism*
  • Protein Binding
  • Protein Kinase C / metabolism*
  • Receptors for Activated C Kinase
  • Receptors, Cell Surface / metabolism*
  • Recombinant Proteins / metabolism
  • Schizosaccharomyces / metabolism*
  • Schizosaccharomyces pombe Proteins
  • Signal Transduction*

Substances

  • Actins
  • Receptors for Activated C Kinase
  • Receptors, Cell Surface
  • Recombinant Proteins
  • Schizosaccharomyces pombe Proteins
  • cpc2 protein, S pombe
  • Protein Kinase C