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Effects of crosstalks between sumoylation and phosphorylation in normal cellular physiology and human diseases

  • Q. Nie
  • , X. D. Gong
  • , M. Liu
  • , D. W.C. Li*
  • *Corresponding author for this work
  • Sun Yat-Sen University
  • Huazhong University of Science and Technology

Research output: Contribution to journalReview articlepeer-review

Abstract

Post-translational modifications (PTMs) such as phosphorylation, acetylation, methylation, ubiquitylation, sumoylation are important mechanisms to regulate functions of different proteins. Among various PTMs, phosphorylation, discovered about 60 years ago, is probably the most common modification. In contrast, sumoylation, identified about two decades ago is emerging as a key regulatory mechanism modulating protein functions. Although studies on protein phosphorylation and sumoylation have been extensively reviewed, much less attention has been paid to their cross-talk and their co-regulation of the same protein target. Here we summarize various examples of the cross-talks between protein phosphorylation and sumoylation, and discuss their functions in regulating normal physiology and pathogenesis.

Original languageEnglish
Pages (from-to)906-913
Number of pages8
JournalCurrent Molecular Medicine
Volume16
Issue number10
DOIs
StatePublished - 1 Dec 2016
Externally publishedYes

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

  1. SDG 3 - Good Health and Well-being
    SDG 3 Good Health and Well-being

Keywords

  • PTM
  • Phosphorylation
  • Protein functions
  • Sumoylation

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