SUMOylation is required for PIPK1γ-driven keratinocyte migration and growth

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In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells
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In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells

Published on: November 2, 2017

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Wei Ni1,2,3, Ying Li4, Lili Cai1

  • 1Cancer Institute of Traditional Chinese Medicine, Longhua Hospital, Shanghai University of Traditional Chinese Medicine, China.

The FEBS Journal
|July 6, 2019
PubMed

Insights

Phosphatidylinositol 4-phosphate kinase (PIPKI) gamma is SUMOylated at Lys-591, which is essential for PIPKI gamma-driven keratinocyte migration and growth. This SUMOylation regulates intracellular PIP2 generation, impacting wound repair.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Phosphatidylinositol 4-phosphate kinase (PIPKI) gamma regulates PIP2 generation, impacting cell functions.
  • PIPKI gamma's role in tumor and nerve cells is known, but its regulation is unclear.

Purpose of the Study:

  • To investigate the regulatory mechanism of PIPKI gamma.
  • To identify novel interactions and modifications of PIPKI gamma.

Main Methods:

  • In vivo and in vitro SUMOylation assays.
  • Identification of SUMO-acceptor sites using site-directed mutagenesis.
  • Assessment of PIPKI gamma function in keratinocyte migration and growth assays.

Main Results:

  • PIPKI gamma specifically associates with UBC9 and undergoes SUMOylation.
  • Lys-591 was identified as the critical SUMO-acceptor site for PIPKI gamma.
  • SUMOylation at Lys-591 is crucial for PIPKI gamma-mediated keratinocyte migration, growth, and PIP2 generation.

Conclusions:

  • PIPKI gamma is a novel SUMOylation target.
  • SUMOylation of PIPKI gamma at Lys-591 is essential for keratinocyte function and PIP2 generation.
  • This finding provides insights into wound repair mechanisms.
Keywords:
PIP2PIPKIγSUMOylationkeratinocytepost-translational modification

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