RT Journal Article
SR Electronic
T1 The metabolite-controlled ubiquitin conjugase Ubc8 promotes mitochondrial protein import
JF Life Science Alliance
JO Life Sci. Alliance
FD Life Science Alliance LLC
SP e202201526
DO 10.26508/lsa.202201526
VO 6
IS 1
A1 Saskia Rödl
A1 Fabian den Brave
A1 Markus Räschle
A1 Büsra Kizmaz
A1 Svenja Lenhard
A1 Carina Groh
A1 Hanna Becker
A1 Jannik Zimmermann
A1 Bruce Morgan
A1 Elke Richling
A1 Thomas Becker
A1 Johannes M Herrmann
YR 2023
UL https://www.life-science-alliance.org/content/6/1/e202201526.abstract
AB Mitochondria play a key role in cellular energy metabolism. Transitions between glycolytic and respiratory conditions induce considerable adaptations of the cellular proteome. These metabolism-dependent changes are particularly pronounced for the protein composition of mitochondria. Here, we show that the yeast cytosolic ubiquitin conjugase Ubc8 plays a crucial role in the remodeling process when cells transition from respiratory to fermentative conditions. Ubc8 is a conserved and well-studied component of the catabolite control system that is known to regulate the stability of gluconeogenic enzymes. Unexpectedly, we found that Ubc8 also promotes the assembly of the translocase of the outer membrane of mitochondria (TOM) and increases the levels of its cytosol-exposed receptor subunit Tom22. Ubc8 deficiency results in compromised protein import into mitochondria and reduced steady-state levels of mitochondrial proteins. Our observations show that Ubc8, which is controlled by the prevailing metabolic conditions, promotes the switch from glucose synthesis to glucose usage in the cytosol and induces the biogenesis of the mitochondrial TOM machinery to improve mitochondrial protein import during phases of metabolic transition.