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Dishevelled-KSRP complex regulates Wnt signaling through post-transcriptional stabilization of beta-catenin mRNA

Rama Kamesh Bikkavilli1, Craig C Malbon

  • 1Department of Pharmacology, Health Sciences Center, State University of New York at Stony Brook, Stony Brook, NY 11794-8651, USA. kamesh@pharm.stonybrook.edu

Journal of Cell Science
|March 25, 2010
PubMed

Insights

K-homology splicing regulator protein (KSRP) interacts with Dishevelled proteins to regulate Wnt/beta-catenin signaling. This interaction impacts beta-catenin mRNA stability, affecting embryonic development.

Area of Science:

  • Molecular Biology
  • Developmental Biology
  • Cell Signaling

Background:

  • Canonical Wnt/beta-catenin signaling is essential for embryonic development.
  • Dishevelled proteins act as signal transducers in the Wnt pathway, linking Frizzled receptors to downstream targets.
  • Dysregulation of Wnt signaling is implicated in various developmental abnormalities and diseases.

Purpose of the Study:

  • To identify novel proteins that interact with Dishevelled.
  • To elucidate the role of K-homology splicing regulator protein (KSRP) in Wnt/beta-catenin signaling.
  • To investigate the mechanism by which KSRP influences beta-catenin expression.

Main Methods:

  • Affinity purification coupled with ion-trap mass spectrometry to identify Dishevelled-interacting proteins.
  • Analysis of CTNNB1 (beta-catenin) mRNA stability.
  • Investigating the formation and function of Dishevelled-KSRP complexes.

Main Results:

  • KSRP was identified as a novel Dishevelled-interacting protein.
  • KSRP negatively regulates Wnt/beta-catenin signaling.
  • KSRP affects the post-transcriptional stability of CTNNB1 (beta-catenin) mRNA.

Conclusions:

  • The Dishevelled-KSRP complex plays a role in Wnt pathway regulation.
  • KSRP's function in Wnt signaling is mediated by controlling beta-catenin mRNA stability post-transcriptionally.
  • This finding reveals a new regulatory mechanism in Wnt signaling crucial for development.

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