TMEM67, TMEM237, and Embigin in Complex With Monocarboxylate Transporter MCT1 Are Unique Components of the Photoreceptor Outer Segment Plasma Membrane.


Journal

Molecular & cellular proteomics : MCP
ISSN: 1535-9484
Titre abrégé: Mol Cell Proteomics
Pays: United States
ID NLM: 101125647

Informations de publication

Date de publication:
2021
Historique:
received: 08 12 2020
revised: 25 03 2021
accepted: 26 04 2021
pubmed: 3 5 2021
medline: 22 3 2022
entrez: 2 5 2021
Statut: ppublish

Résumé

The outer segment (OS) organelle of vertebrate photoreceptors is a highly specialized cilium evolved to capture light and initiate light response. The plasma membrane which envelopes the OS plays vital and diverse roles in supporting photoreceptor function and health. However, little is known about the identity of its protein constituents, as this membrane cannot be purified to homogeneity. In this study, we used the technique of protein correlation profiling to identify unique OS plasma membrane proteins. To achieve this, we used label-free quantitative MS to compare relative protein abundances in an enriched preparation of the OS plasma membrane with a preparation of total OS membranes. We have found that only five proteins were enriched at the same level as previously validated OS plasma membrane markers. Two of these proteins, TMEM67 and TMEM237, had not been previously assigned to this membrane, and one, embigin, had not been identified in photoreceptors. We further showed that embigin associates with monocarboxylate transporter MCT1 in the OS plasma membrane, facilitating lactate transport through this cellular compartment.

Identifiants

pubmed: 33933680
pii: S1535-9476(21)00061-X
doi: 10.1016/j.mcpro.2021.100088
pmc: PMC8167285
pii:
doi:

Substances chimiques

Membrane Proteins 0
Monocarboxylic Acid Transporters 0
Symporters 0
monocarboxylate transport protein 1 0

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Pagination

100088

Subventions

Organisme : NEI NIH HHS
ID : F32 EY029929
Pays : United States
Organisme : NEI NIH HHS
ID : P30 EY005722
Pays : United States
Organisme : NEI NIH HHS
ID : R01 EY002422
Pays : United States
Organisme : NEI NIH HHS
ID : R01 EY030451
Pays : United States
Organisme : NEI NIH HHS
ID : R01 EY026525
Pays : United States
Organisme : NEI NIH HHS
ID : R01 EY012042
Pays : United States
Organisme : NEI NIH HHS
ID : R21 EY027484
Pays : United States
Organisme : NEI NIH HHS
ID : R56 EY012042
Pays : United States

Informations de copyright

Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Conflict of interest The authors declare no competing interests.

Auteurs

Nikolai P Skiba (NP)

Albert Eye Research Institute, Duke University Medical Center, Durham, North Carolina, USA. Electronic address: nikolai.skiba@duke.edu.

Martha A Cady (MA)

Albert Eye Research Institute, Duke University Medical Center, Durham, North Carolina, USA.

Laurie Molday (L)

Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia, Canada.

John Y S Han (JYS)

Department of Pathology, Anatomy, and Cell Biology, Thomas Jefferson University, Philadelphia, Pennsylvania, USA.

Tylor R Lewis (TR)

Albert Eye Research Institute, Duke University Medical Center, Durham, North Carolina, USA.

William J Spencer (WJ)

Albert Eye Research Institute, Duke University Medical Center, Durham, North Carolina, USA.

Will J Thompson (WJ)

Duke Proteomics and Metabolomics Shared Resource, Duke University, Durham, North Carolina, USA.

Sarah Hiles (S)

Duke Proteomics and Metabolomics Shared Resource, Duke University, Durham, North Carolina, USA.

Nancy J Philp (NJ)

Department of Pathology, Anatomy, and Cell Biology, Thomas Jefferson University, Philadelphia, Pennsylvania, USA.

Robert S Molday (RS)

Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia, Canada.

Vadim Y Arshavsky (VY)

Albert Eye Research Institute, Duke University Medical Center, Durham, North Carolina, USA. Electronic address: vadim.arshavsky@duke.edu.

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Classifications MeSH