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Gli Phosphorylation Code in Hedgehog Signal Transduction.

Mengmeng Zhou1, Jin Jiang1,2

  • 1Department of Molecular Biology, UT Southwestern Medical Center, Dallas, TX, United States.

Frontiers in Cell and Developmental Biology
|February 21, 2022
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Summary

Hedgehog (Hh) signaling controls development and tissue health. This review details how phosphorylation of Cubitus interruptus (Ci)/Gli transcription factors by various kinases regulates Hh pathway activity, impacting disease.

Keywords:
CK1CiFuGSK3GliHedgehogPKAUlk3

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Area of Science:

  • Molecular Biology
  • Developmental Biology
  • Cell Signaling

Background:

  • The Hedgehog (Hh) signaling pathway is crucial for embryonic development and tissue homeostasis.
  • Dysregulation of Hh signaling is linked to human diseases like cancer and birth defects.
  • The pathway's core mechanism involves regulating the transcription factor Cubitus interruptus (Ci)/Gli.

Purpose of the Study:

  • To review the regulation of Ci/Gli phosphorylation events.
  • To elucidate how these phosphorylation events influence Hh signal transduction.
  • To provide an updated understanding of Hh pathway regulation.

Main Methods:

  • Review of existing literature on Hh signaling and Ci/Gli phosphorylation.
  • Analysis of the roles of various kinases (PKA, GSK3, CK1, Fu/Ulk3/Stk36) in Ci/Gli regulation.
  • Examination of the interplay between phosphorylation, protein processing, and pathway activation.

Main Results:

  • Sequential phosphorylation by PKA, GSK3, and CK1 generates the repressor form (CiR/GliR) via proteolytic processing.
  • Phosphorylation by Fused (Fu)/Unc-51 like kinase (Ulk) family kinases (Fu/Ulk3/Stk36) promotes the activator form (CiA/GliA).
  • Hh stimulation enhances Fu/Ulk3/Stk36-mediated phosphorylation, altering Ci/Gli interaction with Sufu.

Conclusions:

  • Phosphorylation is a key regulatory mechanism controlling Ci/Gli activity in the Hh pathway.
  • Distinct phosphorylation events dictate whether Ci/Gli acts as a repressor or activator.
  • Understanding these phosphorylation dynamics is vital for deciphering Hh pathway function and therapeutic targeting.