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Skiba NP, Cady MA, Molday L, et al. TMEM67, TMEM237, and Embigin in Complex With Monocarboxylate Transporter MCT1 Are Unique Components of the Photoreceptor Outer Segment Plasma Membrane. Mol Cell Proteomics. 2021;20:100088doi: 10.1016/j.mcpro.2021.100088.
Skiba, N. P., Cady, M. A., Molday, L., Han, J. Y. S., Lewis, T. R., Spencer, W. J., Thompson, W. J., Hiles, S., Philp, N. J., Molday, R. S., & Arshavsky, V. Y. (2021). TMEM67, TMEM237, and Embigin in Complex With Monocarboxylate Transporter MCT1 Are Unique Components of the Photoreceptor Outer Segment Plasma Membrane. Molecular & cellular proteomics : MCP, 20100088. https://doi.org/10.1016/j.mcpro.2021.100088
Skiba, Nikolai P, et al. "TMEM67, TMEM237, and Embigin in Complex With Monocarboxylate Transporter MCT1 Are Unique Components of the Photoreceptor Outer Segment Plasma Membrane." Molecular & cellular proteomics : MCP vol. 20 (2021): 100088. doi: https://doi.org/10.1016/j.mcpro.2021.100088
Skiba NP, Cady MA, Molday L, Han JYS, Lewis TR, Spencer WJ, Thompson WJ, Hiles S, Philp NJ, Molday RS, Arshavsky VY. TMEM67, TMEM237, and Embigin in Complex With Monocarboxylate Transporter MCT1 Are Unique Components of the Photoreceptor Outer Segment Plasma Membrane. Mol Cell Proteomics. 2021 Apr 30;20:100088. doi: 10.1016/j.mcpro.2021.100088. Epub 2021 Apr 30. PMID: 33933680; PMCID: PMC8167285.
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Mol Cell Proteomics. 2021 Apr 30;20:100088. doi: 10.1016/j.mcpro.2021.100088. Epub 2021 Apr 30.

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

Molecular & cellular proteomics : MCP

Nikolai P Skiba, Martha A Cady, Laurie Molday, John Y S Han, Tylor R Lewis, William J Spencer, Will J Thompson, Sarah Hiles, Nancy J Philp, Robert S Molday, Vadim Y Arshavsky

Affiliations

  1. Albert Eye Research Institute, Duke University Medical Center, Durham, North Carolina, USA. Electronic address: [email protected].
  2. Albert Eye Research Institute, Duke University Medical Center, Durham, North Carolina, USA.
  3. Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia, Canada.
  4. Department of Pathology, Anatomy, and Cell Biology, Thomas Jefferson University, Philadelphia, Pennsylvania, USA.
  5. Duke Proteomics and Metabolomics Shared Resource, Duke University, Durham, North Carolina, USA.
  6. Albert Eye Research Institute, Duke University Medical Center, Durham, North Carolina, USA. Electronic address: [email protected].

PMID: 33933680 PMCID: PMC8167285 DOI: 10.1016/j.mcpro.2021.100088

Abstract

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.

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

Keywords: lactate transport; photoreceptor; plasma membrane; protein correlation profiling; retina

Conflict of interest statement

Conflict of interest The authors declare no competing interests.

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