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Article

Distinct functional modes of SUMOylation for retinoid X receptor alpha.

Biochemical and biophysical research communications - 14 Aug 2015

Lee Wai-Ping, Jena Sarita, Rodriguez E Patricia, O'Donovan Sinead P, Wagner Carl, Jurutka Peter W, Thompson Paul D

Abstract excerpt

The present study investigated human retinoid X receptor alpha (hRXRα) as a substrate for modification with small ubiquitin like modifier (SUMO) and how members of the protein inhibitor of activated STAT (PIAS) family may impact upon this process. In agreement with a previous study, we validate Ubc9 to facilitate SUMOylation of hRXRα at lysine 108 but note this modification to occur for all isoforms rather than...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 26116533
DOI: 10.1016/j.bbrc.2015.06.115

Genes

PIAS4
SUMO1
SUMO2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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