Co-adaptor driven assembly of a CUL3 E3 ligase complex.

Adaptor Proteins, Signal Transducing / genetics Calcium-Binding Proteins / genetics Cullin Proteins / genetics HEK293 Cells Humans Mannosyltransferases / genetics Membrane Proteins / genetics Protein Binding Protein Interaction Domains and Motifs Protein Stability Ubiquitin Thiolesterase / genetics Ubiquitination
ALG2 CAND1 CUL3 KLHL12 PEF1 SEC31 adaptor exchange monoubiquitylation ubiquitin

Journal

Molecular cell
ISSN: 1097-4164
Titre abrégé: Mol Cell
Pays: United States
ID NLM: 9802571

Informations de publication

Date de publication:
03 02 2022
Historique:
received: 02 08 2021
revised: 16 11 2021
accepted: 06 01 2022
entrez: 5 2 2022
pubmed: 6 2 2022
medline: 1 3 2022
Statut: ppublish

Résumé

Cullin-RING E3 ligases (CRLs) are essential ubiquitylation enzymes that combine a catalytic core built around cullin scaffolds with ∼300 exchangeable substrate adaptors. To ensure robust signal transduction, cells must constantly form new CRLs by pairing substrate-bound adaptors with their cullins, but how this occurs at the right time and place is still poorly understood. Here, we show that formation of individual CRL complexes is a tightly regulated process. Using CUL3

Identifiants

DOI: 10.1016/j.molcel.2022.01.004 PMID: 35120648 PMC: PMC8884472
pubmed: 35120648
pii: S1097-2765(22)00004-1
doi: 10.1016/j.molcel.2022.01.004
pmc: PMC8884472
mid: NIHMS1776276
pii:
doi:

Substances chimiques

Adaptor Proteins, Signal Transducing 0
CUL3 protein, human 0
Calcium-Binding Proteins 0
Cullin Proteins 0
KLHL12 protein, human 0
LNPK protein, human 0
Membrane Proteins 0
PEF1 protein, human 0
USP9X protein, human 0
Mannosyltransferases EC 2.4.1.-
Ubiquitin Thiolesterase EC 3.4.19.12

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S.

Langues

eng

Sous-ensembles de citation

IM

Pagination

585-597.e11

Subventions

Organisme : NIGMS NIH HHS
ID : F32 GM123716
Pays : United States

Informations de copyright

Copyright © 2022 The Authors. Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of interests M.R. is a founder and member of the scientific advisory board of Nurix Therapeutics; a scientific advisory board member of Monte Rosa Therapeutics; an iPartner of The Column Group; and a member of the advisory board of Molecular Cell.

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Auteurs

David Akopian (D)

Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley CA 94720, USA.

Colleen A McGourty (CA)

Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley CA 94720, USA.

Michael Rapé (M)

Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley CA 94720, USA; Howard Hughes Medical Institute, University of California at Berkeley, Berkeley CA 94720, USA; Quantitative Biosciences Institute, QB3, University of California at Berkeley, Berkeley CA 94720, USA. Electronic address: mrape@berkeley.edu.

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Classifications MeSH

questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Protéines adaptatrices de la transduction du signal › Co-adaptor driven assembly of a CUL3 E3 ligase complex.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines de transport › Protéines de liaison au calcium › Co-adaptor driven assembly of a CUL3 E3 ligase complex.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines du cycle cellulaire › Cullines › Co-adaptor driven assembly of a CUL3 E3 ligase complex.
questionsmedicales.fr › Cellules › Cellules épithéliales › Cellules HEK293 › Co-adaptor driven assembly of a CUL3 E3 ligase complex.
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › Co-adaptor driven assembly of a CUL3 E3 ligase complex.
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Transferases › Glycosyltransferase › Hexosyltransferases › Mannosyltransferases › Co-adaptor driven assembly of a CUL3 E3 ligase complex.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines membranaires › Co-adaptor driven assembly of a CUL3 E3 ligase complex.
questionsmedicales.fr › Métabolisme › Liaison aux protéines › Co-adaptor driven assembly of a CUL3 E3 ligase complex.
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Éléments structuraux des protéines › Motifs et domaines d'intéraction protéique › Co-adaptor driven assembly of a CUL3 E3 ligase complex.
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Stabilité protéique › Co-adaptor driven assembly of a CUL3 E3 ligase complex.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines associées à la maladie de Parkinson › Ubiquitin thiolesterase › Co-adaptor driven assembly of a CUL3 E3 ligase complex.
questionsmedicales.fr › Phénomènes génétiques › Régulation de l'expression des gènes › Modification traductionnelle des protéines › Maturation post-traductionnelle des protéines › Ubiquitination › Co-adaptor driven assembly of a CUL3 E3 ligase complex.