A general strategy for discovery of inhibitors and activators of RING and U-box E3 ligases with ubiquitin variants

M Gabrielsen, L Buetow, MA Nakasone, SF Ahmed… - Molecular cell, 2017 - cell.com
Summary RING and U-box E3 ubiquitin ligases regulate diverse eukaryotic processes and
have been implicated in numerous diseases, but targeting these enzymes remains a major …

N‐Terminally extended human ubiquitin‐conjugating enzymes (E2s) mediate the ubiquitination of RING‐finger proteins, ARA54 and RNF8

K Ito, S Adachi, R Iwakami, H Yasuda… - European Journal of …, 2001 - Wiley Online Library
We have previously cloned cDNAs encoding the N‐terminally extended class III human
ubiquitin‐conjugating enzymes (E2s), UBE2E2 and UBE2E3, the biological functions of …

RING E3-catalyzed E2 self-ubiquitination attenuates the activity of Ube2E ubiquitin-conjugating enzymes

PA Banka, AP Behera, S Sarkar, AB Datta - Journal of molecular biology, 2015 - Elsevier
Ubiquitination of a target protein is accomplished through sequential actions of the E1, E2s,
and the E3s. E2s dictate the modification topology while E3 ligases confer substrate …

A UbcH5/ubiquitin noncovalent complex is required for processive BRCA1-directed ubiquitination

PS Brzovic, A Lissounov, DE Christensen, DW Hoyt… - Molecular cell, 2006 - cell.com
Protein ubiquitination is a powerful regulatory modification that influences nearly every
aspect of eukaryotic cell biology. The general pathway for ubiquitin (Ub) modification …

Ubiquitin transfer from the E2 perspective: why is UbcH5 so promiscuous?

PS Brzovic, RE Klevit - Cell cycle, 2006 - Taylor & Francis
Protein ubiquitination is a regulatory process that influences nearly every aspect of
eukaryotic cell biology. Pathways that range from cell-cycle progression and differentiation …

An unusual transmembrane helix in the endoplasmic reticulum ubiquitin ligase Doa10 modulates degradation of its cognate E2 enzyme

SG Kreft, M Hochstrasser - Journal of Biological Chemistry, 2011 - ASBMB
In the endoplasmic reticulum (ER), nascent membrane and secreted proteins that are
misfolded are retrotranslocated into the cytosol and degraded by the proteasome. For most …

Expression, purification, and properties of the Ubc4/5 family of E2 enzymes

KL Lorick, JP Jensen, AM Weissman - Methods in enzymology, 2005 - Elsevier
Ubiquitin‐conjugating enzymes (E2s) play a central role in ubiquitylation. They function to
bridge the first, nonspecific step of ubiquitin activation by E1 with the transfer of activated …

Ubiquitin in motion: structural studies of the ubiquitin-conjugating enzyme∼ ubiquitin conjugate

JN Pruneda, KE Stoll, LJ Bolton, PS Brzovic… - Biochemistry, 2011 - ACS Publications
Ubiquitination of proteins provides a powerful and versatile post-translational signal in the
eukaryotic cell. The formation of a thioester bond between ubiquitin (Ub) and the active site …

[HTML][HTML] The E2–E3 interaction in the N-end rule pathway: the RING-H2 finger of E3 is required for the synthesis of multiubiquitin chain

Y Xie, A Varshavsky - The EMBO journal, 1999 - embopress.org
We dissected physical and functional interactions between the ubiquitin-conjugating (E2)
enzyme Ubc2p and Ubr1p, the E3 component of the N-end rule pathway in Saccharomyces …

Characterization of RING-between-RING E3 ubiquitin transfer mechanisms

KH Reiter, RE Klevit - The Ubiquitin Proteasome System: Methods and …, 2018 - Springer
Protein ubiquitination is an essential posttranslational modification that regulates nearly all
cellular processes. E3 ligases catalyze the final transfer of ubiquitin (Ub) onto substrates and …