Membrane orientation and oligomerization of the melanocortin receptor accessory protein 2.

G protein–coupled receptor (GPCR) accessory protein melanocortin receptor membrane protein membrane threading metabolic regulation obesity transmembrane domain

Journal

The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R

Informations de publication

Date de publication:
27 11 2020
Historique:
received: 03 08 2020
revised: 08 09 2020
pubmed: 19 9 2020
medline: 10 3 2021
entrez: 18 9 2020
Statut: ppublish

Résumé

The melanocortin receptor accessory protein 2 (MRAP2) plays a pivotal role in the regulation of several G protein-coupled receptors that are essential for energy balance and food intake. MRAP2 loss-of-function results in obesity in mammals. MRAP2 and its homolog MRAP1 have an unusual membrane topology and are the only known eukaryotic proteins that thread into the membrane in both orientations. In this study, we demonstrate that the conserved polybasic motif that dictates the membrane topology and dimerization of MRAP1 does not control the membrane orientation and dimerization of MRAP2. We also show that MRAP2 dimerizes through its transmembrane domain and can form higher-order oligomers that arrange MRAP2 monomers in a parallel orientation. Investigating the molecular details of MRAP2 structure is essential for understanding the mechanism by which it regulates G protein-coupled receptors and will aid in elucidating the pathways involved in metabolic dysfunction.

Identifiants

pubmed: 32943551
pii: S0021-9258(17)50456-1
doi: 10.1074/jbc.RA120.015482
pmc: PMC7705299
pii:
doi:

Substances chimiques

Adaptor Proteins, Signal Transducing 0
MRAP2 protein, human 0

Types de publication

Journal Article Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

16370-16379

Subventions

Organisme : NIDDK NIH HHS
ID : P30 DK020572
Pays : United States
Organisme : NIDDK NIH HHS
ID : R01 DK070332
Pays : United States
Organisme : NIDDK NIH HHS
ID : R01 DK110403
Pays : United States

Informations de copyright

© 2020 Chen et al.

Déclaration de conflit d'intérêts

Conflict of interest—The authors declare that they have no conflicts of interest with the contents of this article.

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Auteurs

Valerie Chen (V)

Department of Chemistry and Biochemistry, University of California, Santa Cruz, California, USA.

Antonio E Bruno (AE)

Department of Chemistry and Biochemistry, University of California, Santa Cruz, California, USA.

Laura L Britt (LL)

Department of Chemistry and Biochemistry, University of California, Santa Cruz, California, USA.

Ciria C Hernandez (CC)

Life Sciences Institute and Department of Molecular and Integrative Physiology, University of Michigan, Ann Arbor, Michigan, USA.

Luis E Gimenez (LE)

Life Sciences Institute and Department of Molecular and Integrative Physiology, University of Michigan, Ann Arbor, Michigan, USA.

Alys Peisley (A)

Life Sciences Institute and Department of Molecular and Integrative Physiology, University of Michigan, Ann Arbor, Michigan, USA.

Roger D Cone (RD)

Life Sciences Institute and Department of Molecular and Integrative Physiology, University of Michigan, Ann Arbor, Michigan, USA.

Glenn L Millhauser (GL)

Department of Chemistry and Biochemistry, University of California, Santa Cruz, California, USA. Electronic address: glennm@ucsc.edu.

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Classifications MeSH