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The UbL protein UBTD1 stably interacts with the UBE2D family of E2 ubiquitin conjugating enzymes

Journal article
Authors Jay Uhler
H. Spahr
G. Farge
S. Clavel
N. G. Larsson
Maria Falkenberg
Tore Samuelsson
Claes M Gustafsson
Published in Biochemical and Biophysical Research Communications
Volume 443
Issue 1
Pages 7-12
ISSN 0006-291X
Publication year 2014
Published at Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages 7-12
Language en
Links dx.doi.org/10.1016/j.bbrc.2013.10.1...
Keywords Ubiquitin, E2 ligase, Proteolysis, Mitochondrion, Ubiquitin-like domain, DENDRITIC CELLS, BINDING DOMAIN, E3 LIGASE, DC-UBP, COMPLEX, DEGRADATION, PROTEASOME, MITOCHONDRIA, MAINTENANCE, MEMBRANE
Subject categories Biochemistry, Cell biology

Abstract

UBTD1 is a previously uncharacterized ubiquitin-like (UbL) domain containing protein with high homology to the mitochondrial Dc-UbP/UBTD2 protein. Here we show that UBTD1 and UBTD2 belong to a family of proteins that is conserved through evolution and found in metazoa, funghi, and plants. To gain further insight into the function of UBTD1, we screened for interacting proteins. In a yeast-2-hybrid (Y2H) screen, we identified several proteins involved in the ubiquitylation pathway, including the UBE2D family of E2 ubiquitin conjugating enzymes. An affinity capture screen for UBTD1 interacting proteins in whole cell extracts also identified members of the UBE2D family. Biochemical characterization of recombinant UBTD1 and UBE2D demonstrated that the two proteins form a stable, stoichiometric complex that can be purified to near homogeneity. We discuss the implications of these findings in light of the ubiquitin proteasome system (UPS). (C) 2013 Published by Elsevier Inc.

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