Determining the Effects of Neddylation on Cullin-RING Ligase-Dependent Protein Ubiquitination.

cullin-RING ligases in vitro assay neddylation protein purification ubiquitination

Journal

Current protocols
ISSN: 2691-1299
Titre abrégé: Curr Protoc
Pays: United States
ID NLM: 101773894

Informations de publication

Date de publication:
Mar 2022
Historique:
entrez: 22 3 2022
pubmed: 23 3 2022
medline: 25 3 2022
Statut: ppublish

Résumé

As the largest family of ubiquitin (Ub) E3 ligases, cullin-RING ligases (CRLs) play crucial roles in various cellular processes, and their activities are tightly regulated by orchestrated mechanisms. Neddylation, the conjugation of a Ub-like protein NEDD8 to a target protein such as the cullin, represents a key regulatory mechanism for CRLs. Biochemical and structural studies of a few CRLs have revealed that cullin neddylation alters the CRL conformation and activates CRL-dependent protein ubiquitination. Here, using CUL2-RING ligase (CRL2) as an example, we describe our protocols for the preparation of recombinant CUL2 with or without NEDD8 conjugation, which is further used to quantitatively determine the effect of neddylation on CRL2-dependent protein ubiquitination in vitro. © 2022 The Authors. Current Protocols published by Wiley Periodicals LLC. Basic Protocol 1: Expression and purification of CUL2•RBX1 from Escherichia coli Support Protocol: Further purification of CUL2•RBX1 with additional chromatography on an FPLC system Basic Protocol 2: Reconstitution of cullin neddylation for quantitative ubiquitination assay in vitro.

Identifiants

pubmed: 35316580
doi: 10.1002/cpz1.401
pmc: PMC8969890
mid: NIHMS1785719
doi:

Substances chimiques

Cullin Proteins 0
Ubiquitin 0
Ubiquitin-Protein Ligases EC 2.3.2.27

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

e401

Subventions

Organisme : American Heart Association-American Stroke Association
ID : 20CDA35270030 - XING LIU
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM138016
Pays : United States
Organisme : NIH HHS
ID : R35GM138016
Pays : United States

Informations de copyright

© 2022 The Authors. Current Protocols published by Wiley Periodicals LLC.

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Auteurs

Kankan Wang (K)

Department of Biochemistry, Purdue University, West Lafayette, Indiana.

Xing Liu (X)

Department of Biochemistry, Purdue University, West Lafayette, Indiana.
Center for Plant Biology, Purdue University, West Lafayette, Indiana.

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Classifications MeSH