Structural and functional analysis of pp70S6k

Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11696-700. doi: 10.1073/pnas.92.25.11696.

Abstract

The pp70/85-kDa S6 kinases, collectively referred to as pp70S6k, are thought to participate in transit through the G1 phase of the cell cycle. pp70S6k regulates the phosphorylation of the 40S ribosomal protein S6 and the transcription factor CREM tau. pp70S6k is regulated by serine/threonine phosphorylation, and although 1-phosphatidylinositol 3-kinase and phospholipase C have been implicated as upstream regulators, the mechanism of activation and identity of the upstream pp70S6k kinases remain unknown. To improve our understanding of how this mitogen-stimulated protein kinase is regulated by growth factors and the immunosuppressant rapamycin, we have initiated a structure/function analysis of pp70S6k. Our results indicate that both the N and C termini participate in the complex regulation of pp70S6k activity.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Androstadienes / pharmacology
  • Animals
  • Cells, Cultured
  • Cricetinae
  • DNA Mutational Analysis
  • Drug Resistance
  • Gene Expression Regulation, Enzymologic
  • Immunosuppressive Agents / pharmacology
  • Mutation
  • Phosphorylation
  • Polyenes / pharmacology
  • Protein Serine-Threonine Kinases / drug effects
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / metabolism*
  • Ribosomal Protein S6 Kinases
  • Sequence Deletion
  • Sirolimus
  • Wortmannin

Substances

  • Androstadienes
  • Immunosuppressive Agents
  • Polyenes
  • Protein Serine-Threonine Kinases
  • Ribosomal Protein S6 Kinases
  • Sirolimus
  • Wortmannin