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Title:
Assembly and Regulation of CRL Ubiquitin Ligases | SpringerLink
Description:
Cullin-RING ubiquitin ligases (CRLs) determine the substrate specificity of ubiquitination reactions, and substrates are recruited to the cullin core through binding to their cognate substrate receptor modules. Because a family of substrate receptors compete for the...
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Keywords {🔍}
pubmed, article, google, scholar, cas, central, cell, protein, ubiquitin, nedd, biol, ligase, mol, neddylation, scf, cullin, ligases, cand, complex, chem, cullinring, cul, nature, regulation, chapter, assembly, liu, ubiquitinlike, arabidopsis, conjugation, modification, commun, activity, structural, pathway, cop, signalosome, biochem, structure, biophys, deshaies, substrate, exchange, enzyme, plant, required, mechanism, res, ubiquitination, proteins,
Topics {✒️}
appbp1-uba3-nedd8-atp complex reveals skp1-cul1-f-box tbp ubiquitin/proteasome-mediated protein degradation skp1-cul1-f-box protein sloper-mould ke month download article/chapter n-terminal acetylation acts scaffold-type e3 ligase cullin-ring catalytic core ran-nucleotide exchange catalyzed cullin–ring e3 networks 120-kda tbp-interacting protein stress-inducible dual e2 chapter cullin-ring ligases conserved protein dcn-1/dcn1p nedd8 recruits e2-ubiquitin ubiquitin c-terminal hydrolases ubiquitin-related protein rub1 unmodified cul1-interacting protein f-box protein expression deconjugating hyper-neddylated cul1 roc1-cul1 complex ubiquitin-activating enzyme e1 huang dt ubp-family deubiquitinating enzyme nedd-cul1 conjugate cleavage cullin-ring ligases skp1-f-box e2-ring expansion scf e3 ligase e2 binding domain ring e3 trapped scf ubiquitin-ligase ubiquitin ligase scf crl ubiquitin ligases ubiquitin pathway enzymes device instant download dual e3 mechanism cand1-dependent remodelling ubiquitin transfer cascade rub/nedd8 conjugation pathway privacy choices/manage cookies scf ubiquitin ligases c-terminal tail fischer es boh bk editor information editors heat-repeat protein cand1-mediated cycling conjugating enzymes
Schema {🗺️}
ScholarlyArticle:
headline:Assembly and Regulation of CRL Ubiquitin Ligases
pageEnd:46
pageStart:33
image:https://media.springernature.com/w153/springer-static/cover/book/978-981-15-1025-0.jpg
genre:
Biomedical and Life Sciences
Biomedical and Life Sciences (R0)
isPartOf:
name:Cullin-RING Ligases and Protein Neddylation
isbn:
978-981-15-1025-0
978-981-15-1024-3
type:Book
publisher:
name:Springer Singapore
logo:
url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
type:ImageObject
type:Organization
author:
name:Kankan Wang
affiliation:
name:Purdue University
address:
name:Department of Biochemistry, Purdue University, West Lafayette, USA
type:PostalAddress
type:Organization
type:Person
name:Raymond J. Deshaies
affiliation:
name:Amgen, One Amgen Center Way
address:
name:Amgen, One Amgen Center Way, Thousand Oaks, USA
type:PostalAddress
type:Organization
type:Person
name:Xing Liu
affiliation:
name:Purdue University
address:
name:Department of Biochemistry, Purdue University, West Lafayette, USA
type:PostalAddress
type:Organization
name:Center for Plant Biology, Purdue University
address:
name:Center for Plant Biology, Purdue University, West Lafayette, USA
type:PostalAddress
type:Organization
email:[email protected]
type:Person
keywords:NEDD8, Neddylation, Cullin, CRLs, SCF, Cand1, Ubiquitination, F-box proteins
description:Cullin-RING ubiquitin ligases (CRLs) determine the substrate specificity of ubiquitination reactions, and substrates are recruited to the cullin core through binding to their cognate substrate receptor modules. Because a family of substrate receptors compete for the same cullin core, the assembly and activity of CRLs are dynamically regulated to fulfill the needs of the cell to adapt to the changing pool of proteins demanding ubiquitination. Cullins are modified by NEDD8, a ubiquitin-like protein. This process, referred to as neddylation, promotes the E3 activity of CRLs by inducing conformational rearrangement in the Cullin-RING catalytic core. Cand1 is a cullin-associated protein whose binding is excluded by cullin neddylation. Although early biochemical studies suggested that Cand1 inhibits CRL activity, genetic studies revealed its positive role in ubiquitination. Emerging evidence from kinetic and quantitative proteomic studies demonstrated that Cand1 stimulates assembly of new Skp1-Cul1-F-box protein (SCF) complexes by exchanging the Skp1-F-box protein substrate receptor modules. Furthermore, aided by refined experimental design as well as computational simulation, an attractive model has been developed in which substrate, neddylation cycle and Cand1-mediated “adaptive exchange” collaborate to maintain the dynamics of the cellular SCF repertoire. Here, we review and discuss recent advances that have deepened our understanding of CRL regulation.
datePublished:2020
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name:Springer Singapore
logo:
url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
type:ImageObject
name:Purdue University
address:
name:Department of Biochemistry, Purdue University, West Lafayette, USA
type:PostalAddress
name:Amgen, One Amgen Center Way
address:
name:Amgen, One Amgen Center Way, Thousand Oaks, USA
type:PostalAddress
name:Purdue University
address:
name:Department of Biochemistry, Purdue University, West Lafayette, USA
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name:Center for Plant Biology, Purdue University
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name:Center for Plant Biology, Purdue University, West Lafayette, USA
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name:Purdue University
address:
name:Department of Biochemistry, Purdue University, West Lafayette, USA
type:PostalAddress
type:Organization
name:Raymond J. Deshaies
affiliation:
name:Amgen, One Amgen Center Way
address:
name:Amgen, One Amgen Center Way, Thousand Oaks, USA
type:PostalAddress
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name:Xing Liu
affiliation:
name:Purdue University
address:
name:Department of Biochemistry, Purdue University, West Lafayette, USA
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name:Center for Plant Biology, Purdue University
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name:Center for Plant Biology, Purdue University, West Lafayette, USA
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email:[email protected]
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name:Department of Biochemistry, Purdue University, West Lafayette, USA
name:Amgen, One Amgen Center Way, Thousand Oaks, USA
name:Department of Biochemistry, Purdue University, West Lafayette, USA
name:Center for Plant Biology, Purdue University, West Lafayette, USA
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