Near-atomic structures of the BBSome reveal the basis for BBSome activation and binding to GPCR cargoes.


Journal

eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614

Informations de publication

Date de publication:
08 06 2020
Historique:
received: 12 02 2020
accepted: 08 06 2020
pubmed: 9 6 2020
medline: 13 3 2021
entrez: 9 6 2020
Statut: epublish

Résumé

Dynamic trafficking of G protein-coupled receptors (GPCRs) out of cilia is mediated by the BBSome. In concert with its membrane recruitment factor, the small GTPase ARL6/BBS3, the BBSome ferries GPCRs across the transition zone, a diffusion barrier at the base of cilia. Here, we present the near-atomic structures of the BBSome by itself and in complex with ARL6

Identifiants

pubmed: 32510327
doi: 10.7554/eLife.55954
pii: 55954
pmc: PMC7311171
doi:
pii:

Substances chimiques

Carrier Proteins 0
Receptors, G-Protein-Coupled 0
Recombinant Proteins 0

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : NIGMS NIH HHS
ID : P41 GM103311
Pays : United States
Organisme : Research to Prevent Blindness
ID : A131667
Pays : International
Organisme : NCRR NIH HHS
ID : M01 RR001271
Pays : United States
Organisme : NIDDK NIH HHS
ID : P30 DK098722
Pays : United States
Organisme : NEI NIH HHS
ID : R01 EY031462
Pays : United States
Organisme : Austrian Science Fund FWF
ID : P 30162
Pays : Austria
Organisme : NIGMS NIH HHS
ID : R01 GM089933
Pays : United States
Organisme : NEI NIH HHS
ID : P30 EY002162
Pays : United States

Informations de copyright

© 2020, Yang et al.

Déclaration de conflit d'intérêts

SY, KB, HC, JW, US, TW, MN No competing interests declared

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Auteurs

Shuang Yang (S)

Laboratory of Molecular Electron Microscopy, The Rockefeller University, New York, United States.

Kriti Bahl (K)

Department of Ophthalmology, University of California San Francisco, San Francisco, United States.

Hui-Ting Chou (HT)

Laboratory of Molecular Electron Microscopy, The Rockefeller University, New York, United States.

Jonathan Woodsmith (J)

Department of Pharmaceutical Chemistry, Institute of Pharmaceutical Sciences, University of Graz and BioTechMed-Graz, Graz, Austria.

Ulrich Stelzl (U)

Department of Pharmaceutical Chemistry, Institute of Pharmaceutical Sciences, University of Graz and BioTechMed-Graz, Graz, Austria.

Thomas Walz (T)

Laboratory of Molecular Electron Microscopy, The Rockefeller University, New York, United States.

Maxence V Nachury (MV)

Department of Ophthalmology, University of California San Francisco, San Francisco, United States.

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