Results 91 to 100 of about 231,680 (303)

Role of E3 ubiquitin ligases in lung cancer

World Journal of Clinical Oncology, 2013
E3 ubiquitin ligases are a large family of proteins that catalyze the ubiquitination of many protein substrates for targeted degradation by the 26S proteasome. Therefore, E3 ubiquitin ligases play an essential role in a variety of biological processes including cell cycle regulation, proliferation and apoptosis.
Snoek, B.C., de Wilt, L.H.A.M., Jansen, G., Peters, G.J.   +3 more
openaire   +2 more sources

Threonine 348 regulates the subcellular localization of PTEN

FEBS Open Bio, EarlyView.
Thr348 in the C2 domain is a key contributor to PTEN subcellular localization. The PTEN350 fragment and PTENA4 accumulated in the nucleus, whereas PTENK13R,A4 predominantly localized to the plasma membrane. In contrast, substitution of Thr348 with Asp (T348D) disrupted these characteristic localization patterns, resulting in predominant cytoplasmic ...
Takashi Kato, Suzu Tanaka, Miyu Ohashi
wiley   +1 more source

Decoys provide a scalable platform for the identification of plant E3 ubiquitin ligases that regulate circadian function

eLife, 2019
The circadian clock relies on regulated degradation of clock proteins to maintain rhythmicity. Despite this, we know few components that mediate protein degradation.
Ann Feke, Wei Liu, Jing Hong, Man-Wah Li, Chin-Mei Lee, Elton K Zhou, Joshua M Gendron   +6 more
doaj   +1 more source

Functional Dissection of a HECT Ubiquitin E3 Ligase

Molecular & Cellular Proteomics, 2008
Ubiquitination is one of the most prevalent protein post-translational modifications in eukaryotes, and its malfunction is associated with a variety of human diseases. Despite the significance of this process, the molecular mechanisms that govern the regulation of ubiquitination remain largely unknown.
Jin-Ying, Lu, Yu-Yi, Lin, Jiang, Qian, Sheng-Ce, Tao, Jian, Zhu, Cecile, Pickart, Heng, Zhu   +6 more
openaire   +2 more sources

The C‐terminal domain of yeast Arginyltransferase1 is essential for its catalytic activity

FEBS Open Bio, EarlyView.
Arginyltransferase 1 (Ate1), a eukaryotic enzyme, catalyses arginylation, transferring arginine from tRNA‐Arg to the amino terminus of the target protein. Overexpression of Ate1 in yeast is lethal and is dependent on arginylation. This study elucidates how mutations in the cofactor‐binding and active site of Ate1 and truncation of its structural ...
Vikas Kumar Yadav, Shweta Shweta, Manisha Malhotra, Vikash Maurya, Akhilesh Kumar   +4 more
wiley   +1 more source

Parkin is protective against proteotoxic stress in a transgenic zebrafish model [PDF]

, 2010
Mutations in the gene encoding the E3 ubiquitin ligase parkin (PARK2) are responsible for the majority of autosomal recessive parkinsonism. Similarly to other knockout mouse models of PD-associated genes, parkin knockout mice do not show a substantial ...
van Bebber Frauke, Dominik Paquet, Winklhofer Konstanze F., Pilsl Anna, Fett, Mareike E., Christian Haass, Bettina Schmid, Anna Pilsl, Mareike E Fett, Frauke van Bebber, Jörg Tatzelt, Fett Mareike E., Paquet, Dominik, Konstanze F. Winklhofer, Schmid Bettina, Paquet Dominik, Haass, Christian, Schmid, Bettina, Tatzelt Jörg, Tatzelt, Jörg, Pilsl, Anna, Konstanze F Winklhofer, Winklhofer, Konstanze F., Haass Christian, Bebber, Frauke van, Mareike E. Fett   +25 more
core   +2 more sources

TRAIP Mediates Alcohol‐Induced Liver Injury through Regulating β‐catenin Ubiquitin Degradation via Direct Interaction

Advanced Science, EarlyView.
This study reveals that NF‐κB1‐driven TRAIP upregulation in ALD correlates with disease severity. Mechanistically, TRAIP directly binds β‐catenin via its CC domain and promotes its K48‐linked ubiquitination and degradation, which is independent of the GSK3β/β‐TrCP pathway.
Zhan Wu, Mingjiang Liu, Lijuan Liao, Zhaohong Mo, Wenli Xu, Linfeng Mao, Yubing Chen, Qiuli Xie, Ming Yao, Shilian Chen, Stephen Tomlinson, Sebastian Mueller, Songqing He, Guandou Yuan   +13 more
wiley   +1 more source

UBE2QL1 is Disrupted by a Constitutional Translocation Associated with Renal Tumor Predisposition and is a Novel Candidate Renal Tumor Suppressor Gene [PDF]

, 2013
Investigation of rare familial forms of renal cell carcinoma (RCC) has led to the identification of genes such as VHL and MET that are also implicated in the pathogenesis of sporadic RCC. In order to identify a novel candidate renal tumor suppressor gene,
Hodgson, S, Morris, Mark R., Turnell, Andrew S., Woodward, ER, Prigmore, Elena, Woodward, Emma R.; id_orcid, Wake, NC, Wake, Naomi C., Gribble, Susan M., Ricketts, Christopher J., Skytte, AB, Brown, Michael, Banks, RE, Morris, MR, Prigmore, E, Maher, ER, Woodward, Emma R., Clarke, Noel, Hodgson, Shirley, Skytte, Anne-bine, Ricketts, CJ, Turnell, AS, Brown, Michael; id_orcid, Maher, Eamonn R., Clarke, N, Banks, Rosamonde E., Gribble, SM, Brown, M, Skytte, Anne Bine, Wake, N, Clarke, Noel W, Brown, Michael D, Ricketts, C, Woodward, E, Skytte, A-B, Maher, E, Morris, M, Banks, R, Turnell, A, Gribble, S   +39 more
core   +1 more source

E3 ubiquitin ligases in signaling, disease, and therapeutics

Trends in Biochemical Sciences
The ubiquitin-proteasome system (UPS) is a central regulator of protein turnover and signaling, with E3 ubiquitin ligases conferring substrate specificity and chain-type control. Recent advances have revealed new mechanistic classes of E3 ligases and expanded our understanding of their roles in disease, including cancer, neurodegeneration, and immune ...
Pirouz Ebadi, Caleb M. Stratton, Shaun K. Olsen   +2 more
openaire   +2 more sources

Microglial Deubiquitinase OTUD7B Stabilizes STAT3 to Promote Neuroinflammation and Cognitive Decline in Alzheimer's Disease

Advanced Science, EarlyView.
. ABSTRACT Neuroinflammation driven by microglial activation is a defining feature of Alzheimer's disease (AD), yet the molecular mechanisms sustaining this proinflammatory state remain unclear. Here, we identify the deubiquitinase OTUD7B as a critical regulator of microglial activation and AD pathology.
Luyao Li, Hao Tang, Qin Yu, Yuyang Zhang, Binglu Shi, Ying Kong, Leiyu Xu, Jingjing Shao, Chenghong Hu, Lingyu She, Zhe Wang, Haiyi Chen, Aleksandr V. Samorodov, Gang Cao, Xia Zhao, Yi Wang   +15 more
wiley   +1 more source