Results 11 to 20 of about 117,949 (359)

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

Detection of sequential polyubiquitylation on a millisecond timescale [PDF]

Nature, 2009
The pathway by which ubiquitin chains are generated on substrate through a cascade of enzymes consisting of an E1, E2 and E3 remains unclear. Multiple distinct models involving chain assembly on E2 or substrate have been proposed.
Deshaies, Raymond J., Kleiger, Gary, Pierce, Nathan W., Shan, Shu-ou   +3 more
core   +3 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

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.
Joanna Liwocha, Jerry Li, Nicholas Purser, Chutima Rattanasopa, Samuel A Maiwald, David T. Krist, D. C. Scott, Barbara Steigenberger, J. R. Prabu, Brenda A. Schulman, Gary Kleiger   +10 more
semanticscholar   +2 more sources

The deubiquitinase Rpn11 functions as an allosteric ubiquitin sensor to promote substrate engagement by the 26S proteasome [PDF]

Cell Reports
Summary: The 26S proteasome is the major compartmental protease in eukaryotic cells, responsible for the ATP-dependent turnover of obsolete, damaged, or misfolded proteins that are delivered for degradation through attached ubiquitin modifications ...
Zaw Min Htet, Ken C. Dong, Andreas Martin   +2 more
doaj   +2 more sources

The E3 ligase RAD18-mediated ubiquitination of henipavirus matrix protein promotes its nuclear-cytoplasmic trafficking and viral egress [PDF]

Emerging Microbes and Infections
The nuclear-cytoplasmic trafficking of matrix proteins (M) is essential for henipavirus budding, with M protein ubiquitination playing a pivotal role in this dynamic process.
Dongning Jin, Linliang Zhang, Cheng Peng, Mingbin He, Weiwei Wang, Zhifei Li, Cong Liu, Jinhong Du, Jin Zhou, Lei Yin, Chao Shan, Yali Qin, Mingzhou Chen   +12 more
doaj   +2 more sources

To Be or Not to Be...Ubiquitinated? [PDF]

Cell Cycle, 2004
Levels of p21, a cyclin-dependent kinase (CDK) inhibitor, are controlled in part at the post-translational level by protein degradation. Although the signaling pathways leading to p21 degradation have not yet been fully elucidated, it is evident that p21 ubiquitination is an essential factor in its degradation.
Michele Pagano, Joanna Bloom
openaire   +3 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

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