Results 111 to 120 of about 308,731 (375)

USP15 regulates dynamic protein-protein interactions of the spliceosome through deubiquitination of PRP31. [PDF]

, 2017
Post-translational modifications contribute to the spliceosome dynamics by facilitating the physical rearrangements of the spliceosome. Here, we report USP15, a deubiquitinating enzyme, as a regulator of protein-protein interactions for the spliceosome ...
Das, Tanuza, Kim, Eunice EunKyeong, Kim, Eunji, Park, Jinyoung, Park, Joon Kyu, Rape, Michael, Song, Eun Joo   +6 more
core   +1 more source

BMI‐1 modulation and trafficking during M phase in diffuse intrinsic pontine glioma

FEBS Open Bio, EarlyView.
The schematic illustrates BMI‐1 phosphorylation during M phase, which triggers its translocation from the nucleus to the cytoplasm. In cycling cells, BMI‐1 functions within the PRC1 complex to mediate H2A K119 monoubiquitination. Following PTC596‐induced M phase arrest, phosphorylated BMI‐1 dissociates from PRC1 and is exported to the cytoplasm via its
Banlanjo Umaru, Deepak Kumar Mishra, Shiva Senthil Kumar, Hao‐Han Pang, Brendan Devine, Komal Khan, Rachid Drissi   +6 more
wiley   +1 more source

The role of ubiquitination in health and disease

MedComm
Ubiquitination is an enzymatic process characterized by the covalent attachment of ubiquitin to target proteins, thereby modulating their degradation, transportation, and signal transduction.
Yan Liao, Wangzheqi Zhang, Yang Liu, Chenglong Zhu, Zui Zou   +4 more
doaj   +1 more source

USP22 controls necroptosis by regulating receptor‐interacting protein kinase 3 ubiquitination

EMBO Reports, 2020
Dynamic control of ubiquitination by deubiquitinating enzymes is essential for almost all biological processes. Ubiquitin‐specific peptidase 22 (USP22) is part of the SAGA complex and catalyzes the removal of mono‐ubiquitination from histones H2A and H2B,
Jens Roedig, Lisa Kowald, Thomas Juretschke, R. Karlowitz, Behnaz Ahangarian Abhari, Heiko Roedig, S. Fulda, Petra Beli, Sjoerd J. L. van Wijk   +8 more
semanticscholar   +1 more source

Meta‐analysis fails to show any correlation between protein abundance and ubiquitination changes

FEBS Open Bio, EarlyView.
We analyzed over 50 published proteomics datasets to explore the relationship between protein levels and ubiquitination changes across multiple experimental conditions and biological systems. Although ubiquitination is often associated with protein degradation, our analysis shows that changes in ubiquitination do not globally correlate with changes in ...
Nerea Osinalde, Unai Alduntzin, Gorka Prieto, Ugo Mayor   +3 more
wiley   +1 more source

Quantitative Analysis of Ubiquitinated Proteins in Human Pituitary and Pituitary Adenoma Tissues

Frontiers in Endocrinology, 2019
Protein ubiquitination is an important post-translational modification that is associated with multiple diseases, including pituitary adenomas (PAs). Protein ubiquitination profiling in human pituitary and PAs remains unknown.
Shehua Qian, Shehua Qian, Shehua Qian, Xiaohan Zhan, Xiaohan Zhan, Xiaohan Zhan, Miaolong Lu, Miaolong Lu, Miaolong Lu, Na Li, Na Li, Na Li, Ying Long, Ying Long, Ying Long, Xuejun Li, Dominic M. Desiderio, Xianquan Zhan, Xianquan Zhan, Xianquan Zhan, Xianquan Zhan   +20 more
doaj   +1 more source

SQSTM1/p62 promotes mitochondrial ubiquitination independently of PINK1 and PRKN/parkin in mitophagy

Autophagy, 2019
The ubiquitination of mitochondrial proteins labels damaged mitochondria for degradation through mitophagy. We recently developed an in vivo system in which mitophagy is slowed by inhibiting mitochondrial division through knockout of Dnm1l/Drp1, a ...
Tatsuya Yamada, T. Dawson, T. Yanagawa, M. Iijima, H. Sesaki   +4 more
semanticscholar   +1 more source

Posttranslational modifications of GLUT4 affect its subcellular localization and translocation [PDF]

, 2013
The facilitative glucose transporter type 4 (GLUT4) is expressed in adipose and muscle and plays a vital role in whole body glucose homeostasis. In the absence of insulin, only ~1% of cellular GLUT4 is present at the plasma membrane, with the vast ...
Bayer, Begum, Birnbaum, Bogan, Bogan, Bogan, Bryant, Cassie Welburn, Chang, Fujita, Garvey, Gill, Giorgino, Govers, Grasbon-Frodl, Gwyn Gould, Haga, Hardy, Herrmann, Hicke, Huang, Ing, James, James, Jessica Sadler, Jeyaraj, Karylowski, Kupriyanova, Lamb, Lau, Lawrence, Lawrence, Leto, Li, Liu, Livingstone, Mahajan, Marsh, Marshall, Marshall, Martin, Matunis, McCormick, Muller, Nia Bryant, Perera, Pessin, Pilch, Piper, Ren, Reusch, Saltiel, Semiz, Shi, Shi, Stöckli, Toh, Urbe, Vannucci, Varki, Watson, Williams, Yang, Yu, Zaarour   +64 more
core   +3 more sources

Patatin‐domain‐containing (phospho)lipases under control: Mammalian co‐regulators and pathogenic activation mechanisms

FEBS Open Bio, EarlyView.
Patatin domain‐containing (phospho)lipases are lipid‐hydrolyzing enzymes central to metabolism, membrane remodeling, and signaling. Their activity relies on precise co‐activation mechanisms involving protein–protein interactions and conformational rearrangements.
Noopur Dubey, Lina Riegler‐Berket, Monika Oberer   +2 more
wiley   +1 more source

Ubiquitination of stalled ribosome triggers ribosome-associated quality control

Nature Communications, 2017
Translation arrest by polybasic sequences induces ribosome stalling, and the arrest product is degraded by the ribosome-mediated quality control (RQC) system. Here we report that ubiquitination of the 40S ribosomal protein uS10 by the E3 ubiquitin ligase
Y. Matsuo, Ken Ikeuchi, Y. Saeki, Shintaro Iwasaki, C. Schmidt, T. Udagawa, Fumiya Sato, Hikaru Tsuchiya, T. Becker, Keiji Tanaka, Nicholas T. Ingolia, R. Beckmann, T. Inada   +12 more
semanticscholar   +1 more source