TORC-SIK cascade regulates CREB activity through the basic leucine zipper domain

FEBS J. 2007 Jul;274(13):3202-9. doi: 10.1111/j.1742-4658.2007.05889.x. Epub 2007 Jun 12.

Abstract

The transcription factor cAMP response element-binding protein (CREB) plays important roles in gene expression induced by cAMP signaling and is believed to be activated when its Ser133 is phosphorylated. However, the discovery of Ser133-independent activation by the activation of transducer of regulated CREB activity coactivators (TORC) and repression by salt inducible kinase cascades suggests that Ser133-independent regulation of CREB is also important. The activation and repression are mediated by the basic leucine zipper domain of CREB. In this review, we focus on the basic leucine zipper domain in the regulation of transcriptional activity of CREB and describe the functions of TORC and salt inducible kinase.

Publication types

  • Review

MeSH terms

  • Animals
  • Cyclic AMP Response Element-Binding Protein / physiology*
  • Cyclic AMP-Dependent Protein Kinases / metabolism
  • Dimerization
  • Humans
  • Leucine Zippers
  • Models, Biological
  • Phosphorylation
  • Protein Structure, Tertiary
  • Protein-Serine-Threonine Kinases / metabolism
  • Serine / chemistry
  • Transcription Factors / metabolism

Substances

  • CRTC1 protein, human
  • Cyclic AMP Response Element-Binding Protein
  • Transcription Factors
  • Serine
  • Protein-Serine-Threonine Kinases
  • SIK1 protein, human
  • Cyclic AMP-Dependent Protein Kinases