Ubiquitination of ERMES components by the E3 ligase Rsp5 is involved in mitophagy - Laboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes
Journal Articles Autophagy Year : 2017

Ubiquitination of ERMES components by the E3 ligase Rsp5 is involved in mitophagy

Abstract

Mitochondria are dynamic organelles that undergo permanent fission and fusion events. These processes play an essential role in maintaining normal cellular function. In the yeast Saccharomyces cerevisiae, the endoplasmic reticulum-mitochondrial encounter structure (ERMES) is a marker of sites of mitochondrial division, but it is also involved in a plethora of other mitochondrial functions. However, it remains unclear how these different functions are regulated. We show here that Mdm34 and Mdm12, 2 components of ERMES, are ubiquitinated by the E3 ligase Rsp5. This ubiquitination is not involved in mitochondrial dynamics or in the distribution and turnover of ERMES. Nevertheless, the ubiquitination of Mdm34 and Mdm12 was required for efficient mitophagy. We thus report here the first identification of ubiquitinated substrates participating in yeast mitophagy.
Fichier principal
Vignette du fichier
Autophagy 2017 Belgareh-Touzé.pdf (2.2 Mo) Télécharger le fichier
Origin Publication funded by an institution
licence

Dates and versions

hal-02401636 , version 1 (02-02-2023)

Licence

Identifiers

Cite

Naïma Belgareh-Touzé, Laetitia Cavellini, Mickaël M Cohen. Ubiquitination of ERMES components by the E3 ligase Rsp5 is involved in mitophagy. Autophagy, 2017, 13 (1), pp.114-132. ⟨10.1080/15548627.2016.1252889⟩. ⟨hal-02401636⟩
43 View
41 Download

Altmetric

Share

More