Results 81 to 90 of about 80,046 (337)

In vitro Auto- and Substrate-Ubiquitination Assays

Bio-Protocol, 2022
The precise regulation of the homeostasis of the cellular proteome is critical for the appropriate growth and development of plants. It also allows the plants to respond to various environmental stresses, by modulating their biochemical and ...
Hye Park, Han Yong Lee, Gyeong Yoon
doaj   +1 more source

USP15 targets ALK3/BMPR1A for deubiquitylation to enhance bone morphogenetic protein signalling [PDF]

, 2014
Protein kinase ALK3/BMPR1A mediates bone morphogenetic protein (BMP) signalling through phosphorylation and activation of SMADs 1/5/8. SMAD6, a transcriptional target of BMP, negatively regulates the BMP pathway by recruiting E3 ubiquitin ligases and ...
Al-Salihi, Mazin A., Bruce, David, Cummins, Timothy D., Dingwell, Kevin S., Ewan, Richard, Herhaus, Lina, Macartney, Thomas, Sapkota, Gopal P., Smith, James C., Vogt, Janis, Wasmus, Lise, Weidlich, Simone   +11 more
core   +3 more sources

RNF38 encodes a nuclear ubiquitin protein ligase that modifies p53

Biochemical and Biophysical Research Communications, 2013
The RNF38 gene encodes a RING finger protein of unknown function. Here we demonstrate that RNF38 is a functional ubiquitin protein ligase (E3). We show that RNF38 isoform 1 is localized to the nucleus by a bipartite nuclear localization sequence (NLS). We confirm that RNF38 is a binding partner of p53 and demonstrate that RNF38 can ubiquitinate p53 in ...
C. Kenneth Kassenbrock, C. Kenneth Kassenbrock, Jamie Sheren   +2 more
openaire   +3 more sources

The E3 ubiquitin ligase, RNF219, suppresses CNOT6L expression to exhibit antiproliferative activity

FEBS Open Bio, EarlyView.
We identified RNF219 as a CCR4‐NOT complex‐interacting E3 ubiquitin ligase that targets the CCR4‐NOT subunit CNOT6L for ubiquitination. RNF219 directly binds to the DUF3819 domain of CNOT1 through its putative α‐helix spanning amino acids 521–542. Our findings also suggest that antiproliferative activity of RNF219 is at least partially mediated by ...
Shou Soeda, Melissa Montrose, Akinori Takahashi, Risa Ishida, Sandrine Burriel, Nao Ohmine, Tohru Natsume, Shungo Adachi, Minsoo Kim, Tadashi Yamamoto   +9 more
wiley   +1 more source

Regulatory role of E3 ubiquitin ligases in multiple myeloma: from molecular mechanisms to therapeutic strategies

Frontiers in Cell and Developmental Biology
Multiple myeloma (MM) is a hematological tumor characterized by the malignant proliferation of plasma cells in bone marrow (BM). Despite the prolonged survival of MM patients, a significant amount of patients relapse or become drug resistant.
Xiaoran Chen, Jiale Zhou, Xiaoqing Dong, Xiaoqing Dong, Yan Xu, Yan Xu, Bing Chen, Bing Chen   +7 more
doaj   +1 more source

Reduced cul-5 activity causes aberrant follicular morphogenesis and germ cell loss in Drosophila oogenesis. [PDF]

PLoS ONE, 2010
Drosophila oogenesis is especially well suited for studying stem cell biology, cellular differentiation, and morphogenesis. The small modifier protein ubiquitin regulates many cellular pathways.
Jan-Michael Kugler, Christopher Lem, Paul Lasko   +2 more
doaj   +1 more source

Hyperglycemia triggers HIPK2 protein degradation [PDF]

, 2016
Homeodomain interacting protein kinase-2 (HIPK2) is an evolutionary conserved kinase that modulates several key molecular pathways to restrain tumor growth and induce p53-depending apoptotic cell-death in response to anticancer therapies. HIPK2 silencing
Baldari, Silvia, Cirone, Mara, Cuomo, Laura, D'Orazi, Gabriella, Garufi, Alessia, Granato, Marisa, Pistritto, Giuseppa   +6 more
core   +2 more sources

A ubiquitin-protein ligase specific for type III protein substrates. [PDF]

Journal of Biological Chemistry, 1990
A previously studied species of ubiquitin-protein ligase contains specific sites for the binding of basic (Type I) and bulky hydrophobic (Type II) NH2-terminal amino acid residues of protein substrates. We now describe another enzyme that ligates ubiquitin specifically to proteins that have NH2-terminal residues other than the above two categories ...
Hannah Heller, A Hershko
openaire   +2 more sources

Overexpression of CDT1 inhibits cell cycle progression at S phase by interacting with the mini‐chromosome maintenance complex and causes DNA damage

FEBS Open Bio, EarlyView.
CDT1 is an essential protein for DNA replication licensing that loads the MCM complex, the eukaryotic replicative DNA helicase, onto replication origins. Overexpression of CDT1 induces cell cycle arrest at the S phase. Here we showed CDT1 inhibits the progression of replication forks by interacting with the MCM complex, leading to the stalling and ...
Takashi Tsuyama, Nonoka Takayama, Rina Tanaka, Yuuki Arai, Yohko Yamaguchi, Yuko Nawata, Yutaro Azuma, Shusuke Tada   +7 more
wiley   +1 more source

Proteasome Lid Bridges Mitochondrial Stress with Cdc53/Cullin1 NEDDylation Status [PDF]

, 2019
Cycles of Cdc53/Cullin1 rubylation (a.k.a NEDDylation) protect ubiquitin-E3 SCF (Skp1-Cullin1-F-box protein) complexes from self-destruction and play an important role in mediating the ubiquitination of key protein substrates involved in cell cycle ...
Bramasole, L., Gefen, E., Glickman, M. H., Gurevich, S., Jimenez-Morales, D., Johnson, J., Klein, Y., Krogan, N. J., Panat, N., Pick, E., Radzinski, M., Reichmann, D., Reis, N., Rinaldi, T., Sinha, A.   +14 more
core   +1 more source