Open AccessAtrogin-1 and MuRF1 regulate cardiac MyBP-C levels via different mechanisms
Author(s) -
Giulia Mearini,
Christina Gedicke,
Saskia Schlossarek,
Christian Witt,
Elisabeth Krämer,
Peirang Cao,
Marcelo D. Gomes,
Stewart H. Lecker,
Siegfried Labeit,
Monte S. Willis,
Thomas Eschenhagen,
Lucie Carrier
Publication year - 2009
Publication title -
cardiovascular research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.774
H-Index - 219
eISSN - 1755-3245
pISSN - 0008-6363
DOI - 10.1093/cvr/cvp348
Subject(s) - ubiquitin , proteasome , mutant , myocyte , ubiquitin ligase , microbiology and biotechnology , biology , ring finger , cardiac muscle , mutation , gene , myh7 , myosin , genetics , endocrinology , myosin light chain kinase
Familial hypertrophic cardiomyopathy (FHC) is frequently caused by cardiac myosin-binding protein C (cMyBP-C) gene mutations, which should result in C-terminal truncated mutants. However, truncated mutants were not detected in myocardial tissue of FHC patients and were rapidly degraded by the ubiquitin-proteasome system (UPS) after gene transfer in cardiac myocytes. Since the diversity and specificity of UPS regulation lie in E3 ubiquitin ligases, we investigated whether the muscle-specific E3 ligases atrogin-1 or muscle ring finger protein-1 (MuRF1) mediate degradation of truncated cMyBP-C.
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