Sumoylation in gene regulation, human disease, and therapeutic action

Xiang Jiao Yang, Cheng Ming Chiang

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

Similar to ubiquitination, sumoylation covalently attaches a small ubiquitin-like modifier (SUMO) protein (92-97 amino acids) to the e-amino group of a lysine residue. This is quite different from the classically defined post-translational modifications, such as phosphorylation, acetylation, and methylation, which typically add a small chemical group to the targeted residue. Sumoylation has been well studied at the molecular and cellular levels, focusing mostly on site-specific conjugation of human SUMO1, SUMO2, and SUMO3, as well as their homologues in various species. In this short review, we will discuss some recent examples to highlight (a) emerging trends about the coordinated regulation of sumoylation and other post-translational modifications in modulating the function of some transcription factors and pathway-specific regulators, (b) diverse roles of sumoylation in gene regulation implicated in stem cells and different pathogenic conditions, and (c) potential therapeutic strategies related to some of the diseases stated above.

Original languageEnglish (US)
JournalF1000Prime Reports
Volume5
DOIs
StatePublished - Nov 1 2013

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Sumoylation
Post Translational Protein Processing
Genes
Ubiquitins
Ubiquitination
Therapeutics
Acetylation
Methylation
Lysine
Transcription Factors
Stem Cells
Phosphorylation
Amino Acids

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Sumoylation in gene regulation, human disease, and therapeutic action. / Yang, Xiang Jiao; Chiang, Cheng Ming.

In: F1000Prime Reports, Vol. 5, 01.11.2013.

Research output: Contribution to journalArticle

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