Results 1 to 10 of about 117,989 (312)

Multiple UBX proteins reduce the ubiquitin threshold of the mammalian p97-UFD1-NPL4 unfoldase

eLife, 2022
The p97/Cdc48 ATPase and its ubiquitin receptors Ufd1-Npl4 are essential to unfold ubiquitylated proteins in many areas of eukaryotic cell biology.
Ryo Fujisawa, Cristian Polo Rivera, Karim PM Labib   +2 more
doaj   +2 more sources

Mechanism of millisecond Lys48-linked poly-ubiquitin chain formation by cullin-RING ligases. [PDF]

Nat Struct Mol Biol
The authors define a NEDD8-activated cullin-RING E3 poly-ubiquitylation mechanism using chemistry, cryo-EM and rapid kinetics. Near-perfect catalytic efficiency is achieved by an E2 ‘synergy loop’ connecting to the E3, donor and acceptor ubiquitins.
Liwocha J, Li J, Purser N, Rattanasopa C, Maiwald S, Krist DT, Scott DC, Steigenberger B, Prabu JR, Schulman BA, Kleiger G.   +10 more
europepmc   +2 more sources

Lys63-linked ubiquitin chain adopts multiple conformational states for specific target recognition

eLife, 2015
A polyubiquitin comprises multiple covalently linked ubiquitins and recognizes myriad targets. Free or bound to ligands, polyubiquitins are found in different arrangements of ubiquitin subunits.
Zhu Liu, Zhou Gong, Wen-Xue Jiang, Ju Yang, Wen-Kai Zhu, Da-Chuan Guo, Wei-Ping Zhang, Mai-Li Liu, Chun Tang   +8 more
doaj   +2 more sources

Neutron-encoded diubiquitins to profile linkage selectivity of deubiquitinating enzymes

Nature Communications, 2023
Most insights into deubiquitinase (DUB) substrate specificity originate from studies with isolated di-ubiquitins (diUb), but in cells diUbs with different linkage types coexist.
Bianca D. M. van Tol, Bjorn R. van Doodewaerd, Guinevere S. M. Lageveen-Kammeijer, Bas C. Jansen, Cami M. P. Talavera Ormeño, Paul J. M. Hekking, Aysegul Sapmaz, Robbert Q. Kim, Angeliki Moutsiopoulou, David Komander, Manfred Wuhrer, Gerbrand J. van der Heden van Noort, Huib Ovaa, Paul P. Geurink   +13 more
doaj   +1 more source

Ubiquitylation functions in the calcium carbonate biomineralization in the extracellular matrix. [PDF]

PLoS ONE, 2012
Mollusks shell formation is mediated by matrix proteins and many of these proteins have been identified and characterized. However, the mechanisms of protein control remain unknown.
Dong Fang, Cong Pan, Huijuan Lin, Ya Lin, Guangrui Xu, Guiyou Zhang, Hongzhong Wang, Liping Xie, Rongqing Zhang   +8 more
doaj   +1 more source

Role of the deubiquitylating enzyme DmUsp5 in coupling ubiquitin equilibrium to development and apoptosis in Drosophila melanogaster. [PDF]

PLoS ONE, 2015
Protein ubiquitylation is a dynamic process that affects the function and stability of proteins and controls essential cellular processes ranging from cell proliferation to cell death. This process is regulated through the balanced action of E3 ubiquitin
Levente Kovács, Olga Nagy, Margit Pál, Andor Udvardy, Octavian Popescu, Péter Deák   +5 more
doaj   +1 more source

Structural snapshots along K48-linked ubiquitin chain formation by the HECT E3 UBR5

bioRxiv, 2023
Ubiquitin chain formation by HECT catalytic domain-containing E3 ligases regulates vast biology, yet the structural mechanisms remain unknown. We employed chemistry and cryo-EM to visualize stable mimics of the intermediates along K48-linked ubiquitin ...
Laura A. Hehl, D. Horn-Ghetko, J. R. Prabu, Ronnald Vollrath, D. Vu, David A. Pérez Berrocal, Monique P. C. Mulder, Gerbrand J. van der Heden van Noort, B. Schulman   +8 more
semanticscholar   +1 more source

Translocation of polyubiquitinated protein substrates by the hexameric Cdc48 ATPase

bioRxiv, 2021
The hexameric Cdc48 ATPase (p97 or VCP in mammals) cooperates with its cofactor Ufd1/Npl4 to extract polyubiquitinated proteins from membranes or macromolecular complexes for degradation by the proteasome.
Zhejian Ji, Hao Li, D. Peterle, J. Paulo, S. Ficarro, T. Wales, J. Marto, S. Gygi, J. Engen, T. Rapoport   +9 more
semanticscholar   +1 more source

Mechanism of selective recognition of Lys48-linked polyubiquitin by macrocyclic peptide inhibitors of proteasomal degradation

Nature Communications, 2023
Post-translational modification of proteins with polyubiquitin chains is a critical cellular signaling mechanism in eukaryotes with implications in various cellular states and processes.
Betsegaw Lemma, Di Zhang, Ganga B. Vamisetti, Bryan G. Wentz, Hiroaki Suga, Ashraf Brik, Jacek Lubkowski, David Fushman   +7 more
doaj   +1 more source

Regulation of the linear ubiquitination of STAT1 controls antiviral interferon signaling

Nature Communications, 2020
LUBAC is involved in adding linear ubiquitin chains to important immune signaling proteins. Here the authors show that this mechanism is effective in inhibiting STAT1-mediated interferon signaling, and that the deubiquitinase OTULIN can remove these ...
Yibo Zuo, Qian Feng, Lincong Jin, Fan Huang, Ying Miao, Jin Liu, Ying Xu, Xiangjie Chen, Hongguang Zhang, Tingting Guo, Yukang Yuan, Liting Zhang, Jun Wang, Hui Zheng   +13 more
doaj   +1 more source