ABIN1 is a signal‐induced autophagy receptor that attenuates NF‐κB activation by recognizing linear ubiquitin chains
Sign Up to like & getrecommendations! Published in 2022 at "FEBS Letters"
DOI: 10.1002/1873-3468.14323
Abstract: Linear ubiquitin chains play pivotal roles in immune signaling by augmenting NF‐κB activation and suppressing programmed cell death induced by various stimuli. A20‐binding inhibitor of NF‐κB 1 (ABIN1) binds to linear ubiquitin chains and attenuates… read more here.
Keywords: autophagy receptor; attenuates activation; ubiquitin chains; linear ubiquitin ... See more keywords
An optical and non‐invasive method to detect the accumulation of ubiquitin chains
Sign Up to like & getrecommendations! Published in 2019 at "Cell Biology International"
DOI: 10.1002/cbin.11186
Abstract: The accumulations of excess amounts of polyubiquitinated proteins are cytotoxic and frequently observed in pathologic tissue from patients of neurodegenerative diseases. Therefore, optical and non‐invasive methods to detect the increase of the amounts of polyubiquitinated… read more here.
Keywords: invasive method; polyubiquitinated proteins; optical non; ubiquitin ... See more keywords
Molecular Recognition of M1-Linked Ubiquitin Chains by Native and Phosphorylated UBAN Domains.
Sign Up to like & getrecommendations! Published in 2019 at "Journal of molecular biology"
DOI: 10.1016/j.jmb.2019.06.012
Abstract: Although the Ub-binding domain in ABIN proteins and NEMO (UBAN) is highly conserved, UBAN-containing proteins exhibit different Ub-binding properties, resulting in their diverse biological roles. Post-translational modifications further control UBAN domain specificity for poly-Ub chains.… read more here.
Keywords: uban domains; recognition linked; molecular recognition; linked chains ... See more keywords
TRIP12 promotes small-molecule-induced degradation through K29/K48-branched ubiquitin chains.
Sign Up to like & getrecommendations! Published in 2021 at "Molecular cell"
DOI: 10.1016/j.molcel.2021.01.023
Abstract: Targeted protein degradation is an emerging therapeutic paradigm. Small-molecule degraders such as proteolysis-targeting chimeras (PROTACs) induce the degradation of neo-substrates by hijacking E3 ubiquitin ligases. Although ubiquitylation of endogenous substrates has been extensively studied, the… read more here.
Keywords: k29 k48; degradation; k48 branched; branched ubiquitin ... See more keywords
An Extended Conformation for K48 Ubiquitin Chains Revealed by the hRpn2:Rpn13:K48-Diubiquitin Structure.
Sign Up to like & getrecommendations! Published in 2020 at "Structure"
DOI: 10.1016/j.str.2020.02.007
Abstract: Rpn13/Adrm1 is recruited to the proteasome by PSMD1/Rpn2, where it serves as a substrate receptor that binds preferentially to K48-linked ubiquitin chains, an established signal for protein proteolysis. Here, we use NMR to solve the… read more here.
Keywords: k48; conformation; structure; k48 diubiquitin ... See more keywords
Branching Out: Improved Signaling by Heterotypic Ubiquitin Chains.
Sign Up to like & getrecommendations! Published in 2019 at "Trends in cell biology"
DOI: 10.1016/j.tcb.2019.06.003
Abstract: Ubiquitin chains of distinct topologies control the stability, interactions, or localization of many proteins in eukaryotic cells, and thus play an essential role in cellular information transfer. It has recently been found that ubiquitin chains… read more here.
Keywords: signaling heterotypic; branching improved; ubiquitin; heterotypic ubiquitin ... See more keywords
Ufd2p synthesizes branched ubiquitin chains to promote the degradation of substrates modified with atypical chains
Sign Up to like & getrecommendations! Published in 2017 at "Nature Communications"
DOI: 10.1038/ncomms14274
Abstract: Ubiquitination of a subset of proteins by ubiquitin chain elongation factors (E4), represented by Ufd2p in Saccharomyces cerevisiae, is a pivotal regulator for many biological processes. However, the mechanism of Ufd2p-mediated ubiquitination is largely unclear.… read more here.
Keywords: substrates modified; degradation; ubiquitin chain; branched ubiquitin ... See more keywords
The activity of TRAF RING homo- and heterodimers is regulated by zinc finger 1
Sign Up to like & getrecommendations! Published in 2017 at "Nature Communications"
DOI: 10.1038/s41467-017-01665-3
Abstract: Ubiquitin chains linked through lysine63 (K63) play a critical role in inflammatory signalling. Following ligand engagement of immune receptors, the RING E3 ligase TRAF6 builds K63-linked chains together with the heterodimeric E2 enzyme Ubc13-Uev1A. Dimerisation… read more here.
Keywords: traf6; zinc finger; activity; ubiquitin chains ... See more keywords
The proteasome 19S cap and its ubiquitin receptors provide a versatile recognition platform for substrates
Sign Up to like & getrecommendations! Published in 2020 at "Nature Communications"
DOI: 10.1038/s41467-019-13906-8
Abstract: Proteins are targeted to the proteasome by the attachment of ubiquitin chains, which are markedly varied in structure. Three proteasome subunits–Rpn10, Rpn13, and Rpn1–can recognize ubiquitin chains. Here we report that proteins with single chains… read more here.
Keywords: chain; degradation; rpn1; ubiquitin receptors ... See more keywords
Central catalytic domain of BRAP (RNF52) recognizes the types of ubiquitin chains and utilizes oligo-ubiquitin for ubiquitylation
Sign Up to like & getrecommendations! Published in 2017 at "Biochemical Journal"
DOI: 10.1042/bcj20161104
Abstract: Really interesting new gene (RING)-finger protein 52 (RNF52), an E3 ubiquitin ligase, is found in eukaryotes from yeast to humans. Human RNF52 is known as breast cancer type 1 susceptibility protein (BRCA1)-associated protein 2 (BRAP… read more here.
Keywords: ubiquitylation; ubiquitin chains; domain; rnf52 domain ... See more keywords
The retracted conformation of ubiquitin Ser65 phosphorylation inhibits the formation of K48-linked ubiquitin chains.
Sign Up to like & getrecommendations! Published in 2022 at "Bioscience reports"
DOI: 10.1042/bsr20220968
Abstract: PINK1, as the first reported ubiquitin kinase, can phosphorylate ubiquitin (Ub) at Ser65 site, which regulates the structure and function of Ub monomer. However, the levels of PINK1 and phosphorylated Ub (pUb) are very low… read more here.
Keywords: k48 linked; ubiquitin ser65; linked ubiquitin; formation k48 ... See more keywords