Inactivation of the VID27 gene prevents suppression of the doa4 degradation defect in doa4Δ did3Δ double mutant.

Biochem Biophys Res Commun

Department of Pharmacology, University of Connecticut Health Center, 263 Farmington Avenue, Farmington, CT, 06030, USA; Institute of Biochemical Physics, Russian Academy of Sciences, 4 Kosygin Street, Moscow, 119991, Russian Federation. Electronic address:

Published: January 2017

Ubiquitination is a key regulatory mechanism that affects numerous cellular processes. This modification is reversible. Deubiquitinating enzymes (DUBs) remove the ubiquitin tag from modified proteins. DUB Doa4 is involved in deubiquitination of conjugates at the late endosome/pre vacuolar compartment. A genetic screen led to isolation of seven extragenic suppressors of the doa4 phenotypic abnormalities. Remarkably, cloned Doa4-independent degradation (DID) genes encode the class E vacuolar protein-sorting factors involved in membrane protein trafficking. Here we provide evidence that inactivation of Vid27 (vacuolar import and degradation) prevents suppression of the doa4 phenotype by did3 mutation. Vid27 is a cytoplasmic protein essential for delivery of fructose-1,6-bisphosphatase into VID vesicles. Thus, our data revealed another connection between Doa4 and vacuolar protein sorting.

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http://dx.doi.org/10.1016/j.bbrc.2016.12.038DOI Listing

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