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Second messenger and Ras/MAPK signalling pathways regulate CLOCK/CYCLE-dependent transcription

Academic Article
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Overview

authors

  • Weber, F.
  • Hung, H. C.
  • Maurer, C.
  • Kay, Steve A.

publication date

  • July 2006

journal

  • Journal of Neurochemistry  Journal

abstract

  • The heterodimeric complex of the transcription factors CLOCK (CLK) and CYCLE (CYC) constitutes the positive element of the circadian clock in Drosophila and mammals. Phosphorylation of clock proteins represents an essential mechanism for promotion and control of the molecular oscillator. However, the kinases and signalling pathways that regulate CLK/CYC function remain largely elusive. In the present study we performed a chemical screen of kinase inhibitors in a cell culture reporter assay to identify functional regulators of CLK/CYC-dependent gene expression. These studies and analysis of constitutively active forms of kinases revealed that cyclic nucleotide/protein kinase A (PKA), calcium/calmodulin-dependent kinase (CaMK) II and Ras/mitogen-activated protein kinase (MAPK) regulate CLK/CYC activity. In vitro phosphorylation analysis showed a direct phosphorylation of CLK by CaMK II and p42 MAPK [extracellular signal-regulated kinase (ERK) 2], suggesting that these kinases regulate CLK/CYC-dependent transcription by direct phosphorylation of CLK.

subject areas

  • ARNTL Transcription Factors
  • Animals
  • Basic Helix-Loop-Helix Transcription Factors
  • CLOCK Proteins
  • Calcium Signaling
  • Dose-Response Relationship, Drug
  • Drosophila
  • Drosophila Proteins
  • Enzyme Inhibitors
  • Gene Expression
  • Gene Expression Regulation
  • Genes, Reporter
  • Luciferases
  • Models, Biological
  • Phosphorylation
  • Signal Transduction
  • Transcription Factors
  • Transcription, Genetic
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Research

keywords

  • Ras
  • behaviour
  • calcium
  • circadian clock
  • cyclic nucleotide
  • mitogen-activated protein kinase
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Identity

International Standard Serial Number (ISSN)

  • 0022-3042

Digital Object Identifier (DOI)

  • 10.1111/j.1471-4159.2006.03865.x

PubMed ID

  • 16805811
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Additional Document Info

start page

  • 248

end page

  • 257

volume

  • 98

issue

  • 1

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