Results 51 to 60 of about 133,567 (215)

The E3 Ubiquitin Ligase MID1 Catalyzes Ubiquitination and Cleavage of Fu [PDF]

Journal of Biological Chemistry, 2014
SHH (Sonic Hedgehog)-GLI signaling plays an important role during embryogenesis and in tumorigenesis. The survival and growth of several types of cancer depend on autonomously activated SHH-GLI signaling. A protein complex containing the ubiquitin ligase MID1 and protein phosphatase 2A regulates the nuclear localization and transcriptional activity of ...
Schweiger, Susann, Dorn, Stephanie, Fuchs, Melanie, Köhler, Andrea, Matthes, Frank, Müller, Eva-Christina, Wanker, Erich, Schneider, Rainer, Krauß, Sybille   +8 more
openaire   +4 more sources

Ub-POD: A Ubiquitin-Specific Proximity-Dependent Labeling Technique to Identify E3 Ubiquitin Ligase Substrates in Human Cells

Bio-Protocol
Ubiquitination is a post-translational protein modification that regulates a vast majority of processes during protein homeostasis. The covalent attachment of ubiquitin is a highly regulated process carried out by the sequential action of the three ...
Urbi Mukhopadhyay, Sophie Levantovsky, Christian Behrends, Sagar Bhogaraju   +3 more
doaj   +1 more source

Regulation of ubiquitin ligase dynamics by the nucleolus [PDF]

The Journal of Cell Biology, 2005
Cellular pathways relay information through dynamic protein interactions. We have assessed the kinetic properties of the murine double minute protein (MDM2) and von Hippel-Lindau (VHL) ubiquitin ligases in living cells under physiological conditions that alter the stability of their respective p53 and hypoxia-inducible factor substrates. Photobleaching
Robert R.J. Hache, Karim Mekhail, Lakshman Gunaratnam, Mireille Khacho, Amanda Carrigan, Stephen Lee   +5 more
openaire   +3 more sources

A pathogen type III effector with a novel E3 ubiquitin ligase architecture.

PLoS Pathogens, 2013
Type III effectors are virulence factors of Gram-negative bacterial pathogens delivered directly into host cells by the type III secretion nanomachine where they manipulate host cell processes such as the innate immunity and gene expression.
Alexander U Singer, Sebastian Schulze, Tatiana Skarina, Xiaohui Xu, Hong Cui, Lennart Eschen-Lippold, Monique Egler, Tharan Srikumar, Brian Raught, Justin Lee, Dierk Scheel, Alexei Savchenko, Ulla Bonas   +12 more
doaj   +1 more source

Synthesis of Isomeric Phosphoubiquitin Chains Reveals that Phosphorylation Controls Deubiquitinase Activity and Specificity

Cell Reports, 2016
Ubiquitin is post-translationally modified by phosphorylation at several sites, but the consequences of these modifications are largely unknown. Here, we synthesize multi-milligram quantities of ubiquitin phosphorylated at serine 20, serine 57, and ...
Nicolas Huguenin-Dezot, Virginia De Cesare, Julien Peltier, Axel Knebel, Yosua Adi Kristaryianto, Daniel T. Rogerson, Yogesh Kulathu, Matthias Trost, Jason W. Chin   +8 more
doaj   +1 more source

Novel Functions of Ubiquitin Ligase HRD1 With Transmembrane and Proline-Rich Domains

Journal of Pharmacological Sciences, 2008
Human ubiquitin ligase HRD1 is involved in endoplasmic reticulum-associated degradation (ERAD). We recently reported that HRD1 interacts with Parkin-associated endothelin receptor-like receptor (Pael-R), a substrate of Parkin, and promotes Pael-R ...
Tomohiro Omura, Masayuki Kaneko, Masayuki Onoguchi, Shinobu Koizumi, Miho Itami, Mariko Ueyama, Yasunobu Okuma, Yasuyuki Nomura   +7 more
doaj  

UFD-2 is an adaptor-assisted E3 ligase targeting unfolded proteins

Nature Communications, 2018
The U-box ubiquitin ligase UFD-2 is one of the most abundant components of the ubiquitin proteasome system in muscle cells. Here the authors perform in vitro and in vivo experiments and show that UFD-2 has E3 ligase activity and that it ubiquitinates ...
Doris Hellerschmied, Max Roessler, Anita Lehner, Linn Gazda, Karel Stejskal, Richard Imre, Karl Mechtler, Alexander Dammermann, Tim Clausen   +8 more
doaj   +1 more source

DTX3L ubiquitin ligase ubiquitinates single-stranded nucleic acids. [PDF]

Elife
AbstractUbiquitination typically involves covalent linking of ubiquitin (Ub) to a lysine residue on a protein substrate. Recently, new facets of this process have emerged, including Ub modification of non-proteinaceous substrates like ADP-ribose by the DELTEX E3 ligase family.
Dearlove EL, Chatrin C, Buetow L, Ahmed SF, Schmidt T, Bushell M, Smith BO, Huang DT.   +7 more
europepmc   +4 more sources

The UAS thioredoxin-like domain of UBXN7 regulates E3 ubiquitin ligase activity of RNF111/Arkadia

BMC Biology, 2023
Background E3 ubiquitin ligases play critical roles in regulating cellular signaling pathways by inducing ubiquitylation of key components. RNF111/Arkadia is a RING E3 ubiquitin ligase that activates TGF-β signaling by inducing ubiquitylation and ...
Sadek Amhaz, Batiste Boëda, Mouna Chouchène, Sabrina Colasse, Florent Dingli, Damarys Loew, Julien Henri, Céline Prunier, Laurence Levy   +8 more
doaj   +1 more source

BRCA1 Is a Histone-H2A-Specific Ubiquitin Ligase

Cell Reports, 2014
The RING domain proteins BRCA1 and BARD1 comprise a heterodimeric ubiquitin (E3) ligase that is required for the accumulation of ubiquitin conjugates at sites of DNA damage and for silencing at DNA satellite repeat regions. Despite its links to chromatin,
Reinhard Kalb, Donna L. Mallery, Conor Larkin, Jeffrey T.J. Huang, Kevin Hiom   +4 more
doaj   +1 more source