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MG53's new identity
Journal article   Open access   Peer reviewed

MG53's new identity

Jennifer R Levy, Kevin P Campbell and David J Glass
Skeletal muscle, Vol.3(1), pp.25-25
11/01/2013
DOI: 10.1186/2044-5040-3-25
PMID: 24175977
url
https://doi.org/10.1186/2044-5040-3-25View
Published (Version of record) Open Access

Abstract

Mitsugumin 53 (MG53) is a relatively newly identified tripartite motif-containing (TRIM) family muscle-specific E3 ubiquitin ligase that is expressed in skeletal muscle and the heart. It has been postulated to facilitate repair by targeting the site of an injury, and acting as a scaffold for assembly of a repair complex made up of dysferlin, annexin V, caveolin-3, and polymerase I and transcript release factor (PTRF). A recent letter published in Nature by Song et al. proposes an alternate function for MG53: as an E3 ligase that targets the insulin receptor and insulin receptor substrate 1 (IRS1) for degradation, therefore regulating muscle insulin signaling. This work is exciting, as it not only presents a novel role for MG53, but also suggests that muscle insulin signaling has a systemic influence on insulin resistance and the metabolic syndrome.

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