Biochemical and Biophysical Research Communications, Vol.482, No.4, 1341-1345, 2017
Inactivation of the VID27 gene prevents suppression of the doa4 degradation defect in doa4 Delta did3 Delta double mutant
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. (C) 2016 Elsevier Inc. All rights reserved.