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- W2227326064 abstract "Cellular quality control provides an efficient surveillance system to regulate mitochondrial turn-over. This study elucidates a novel interaction of the cytosolic E3 ligase, MGRN1 with the ER ubiquitin E3 ligase, GP78. Loss of Mgrn1 function has been implicated in late-onset spongiform neurodegeneration, congenital heart defects amongst several developmental defects. MGRN1 ubiquitinates GP78 in trans via non-canonical K11 linkages. This helps maintain constitutively low levels of GP78 in healthy cells, in turn downregulating mitophagy. GP78, however, does not regulate MGRN1. When mitochondria are stressed, cytosolic Ca2+ increases.This leads to reduced interaction between MGRN1 and GP78 and its compromised ubiquitination. Chelating Ca2+ restores association between the two ligases and the trans ubiquitination. Catalytic inactivation of MGRN1 results in elevated levels of GP78 and consequential increase in the initiation of mitophagy. This is significant because functional depletion of MGRN1 by membrane-associated disease causing prion protein, CtmPrP affects polyubiquitination and degradation of GP78, also leading to an increase in mitophagy events. This suggests that MGRN1 participates in mitochondrial quality control and could contribute to neurodegeneration in a sub-set of CtmPrP mediated prion diseases." @default.
- W2227326064 created "2016-06-24" @default.
- W2227326064 creator A5059944109 @default.
- W2227326064 creator A5075075747 @default.
- W2227326064 date "2016-01-01" @default.
- W2227326064 modified "2023-10-17" @default.
- W2227326064 title "Ubiquitin mediated regulation of the E3 ligase GP78 by Mahogunin in <i>trans</i> affects mitochondrial homeostasis" @default.
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- W2227326064 doi "https://doi.org/10.1242/jcs.176537" @default.
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