The PIK-related kinases intercept conventional signaling pathways

Chem Biol. 1999 May;6(5):R129-36. doi: 10.1016/S1074-5521(99)80070-2.

Abstract

Early efforts to place the first cloned mammalian PIK-related kinase, FRAP, into a conventional membrane to nuclear pathway met with little success. More recent data suggest that members of the family of PIK-related kinases act as intracellular sensors that govern radial and horizontal pathways. These pathways can impinge upon classical membrane to nuclear pathways, as well as components of the cell-cycle machinery.

Publication types

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

MeSH terms

  • Anti-Bacterial Agents / pharmacology
  • Carrier Proteins*
  • Cell Cycle / physiology
  • Cell Nucleus / physiology
  • Humans
  • Immunophilins / metabolism*
  • Phosphatidylinositol 3-Kinases / metabolism
  • Phosphotransferases (Alcohol Group Acceptor)*
  • Signal Transduction*
  • Sirolimus / pharmacology
  • TOR Serine-Threonine Kinases

Substances

  • Anti-Bacterial Agents
  • Carrier Proteins
  • Phosphotransferases (Alcohol Group Acceptor)
  • MTOR protein, human
  • TOR Serine-Threonine Kinases
  • Immunophilins
  • Sirolimus