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Article

The gap junction channel protein connexin 43 is covalently modified and regulated by SUMOylation.

The Journal of biological chemistry - 4 May 2012

Kjenseth Ane, Fykerud Tone A, Sirnes Solveig, Bruun Jarle, Yohannes Zeremariam, Kolberg Matthias, Omori Yasufumi, Rivedal Edgar, Leithe Edward

Abstract excerpt

SUMOylation is a posttranslational modification in which a member of the small ubiquitin-like modifier (SUMO) family of proteins is conjugated to lysine residues in specific target proteins. Most known SUMOylation target proteins are located in the nucleus, but there is increasing evidence that SUMO may also be a key determinant of many extranuclear processes. Gap junctions consist of arrays of intercellular...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 22411987
DOI: 10.1074/jbc.M111.281832
PMCID: PMC3346107

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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The gap junction channel protein connexin 43 is covalently modified and regulated by SUMOylation.PMID 22411987Read ↗

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