Results 91 to 100 of about 223,299 (305)
Unbiased identification of substrates for the Epac1-inducible E3 ubiquitin ligase component SOCS-3
, 2012 The anti-inflammatory effects of the prototypical second messenger cAMP have been extensively documented in multiple cell types. One mechanism by which these effects are achieved is via Epac1 (exchange protein directly activated by cAMP 1)-dependent ...
Williams, Jamie J.L., Palmer, Timothy M.
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FEBS Open Bio, EarlyView.IGFBP4 knockdown (KD) impairs preadipocyte proliferation and is associated with IGF1R protein downregulation and attenuated AKT phosphorylation. The mechanisms by which IGFBP4 KD influences the IGF1R/AKT signaling pathway involve newly synthesized proteins and lysosomal degradation pathways. Created in BioRender.
Yujia Guo +6 more
wiley +1 more source
E3 ubiquitin ligases in T‐cell tolerance [PDF]
European Journal of Immunology, 2009 AbstractThe immune system uses several mechanisms of central and peripheral tolerance in order to prevent the activation of T lymphocytes toward self‐antigens. Although the importance of immune self‐tolerance has been established for a long time, some essential cellular and molecular mechanisms of T‐cell tolerance have only been recently revealed. Once
Magdalena, Paolino, Josef M, Penninger
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FEBS Open Bio, EarlyView.We describe detailed protocols for the purification and preparation of Marchantia polymorpha Auxin Response Factor 2 (MpARF2). This protein is fused to an MBP solubility tag and an mNG fluorescent tag and is purified from Escherichia coli. The presented procedures make it possible to study MpARF2 assemblies, which could arise from phase separation ...
Bas Janssen +5 more
wiley +1 more source
Nature Communications, 2017 Protein stability modulation by E3 ubiquitin ligases is an important layer of functional regulation, but screening for E3 ligase-substrate interactions is time-consuming and costly.
Yang Li +12 more
doaj +1 more source
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 +6 more
doaj +1 more source
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
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. +3 more
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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 +13 more
wiley +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 +6 more
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