Skip to main content

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

Publication ,  Journal Article
Skiba, NP; Cady, MA; Molday, L; Han, JYS; Lewis, TR; Spencer, WJ; Thompson, WJ; Hiles, S; Philp, NJ; Molday, RS; Arshavsky, VY
Published in: Molecular & cellular proteomics : MCP
January 2021

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.

Duke Scholars

Altmetric Attention Stats
Dimensions Citation Stats

Published In

Molecular & cellular proteomics : MCP

DOI

EISSN

1535-9484

ISSN

1535-9476

Publication Date

January 2021

Volume

20

Start / End Page

100088

Related Subject Headings

  • Symporters
  • Retinal Photoreceptor Cell Outer Segment
  • Monocarboxylic Acid Transporters
  • Mice, Inbred C57BL
  • Mice
  • Membrane Proteins
  • Cell Membrane
  • Cattle
  • Biochemistry & Molecular Biology
  • Animals
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Skiba, N. P., Cady, M. A., Molday, L., Han, J. Y. S., Lewis, T. R., Spencer, W. J., … 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, 20, 100088. https://doi.org/10.1016/j.mcpro.2021.100088
Skiba, Nikolai P., Martha A. Cady, Laurie Molday, John Y. S. Han, Tylor R. Lewis, William J. Spencer, Will J. Thompson, 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 20 (January 2021): 100088. https://doi.org/10.1016/j.mcpro.2021.100088.
Skiba NP, Cady MA, Molday L, Han JYS, Lewis TR, Spencer WJ, 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. 2021 Jan;20:100088.
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, Jan. 2021, p. 100088. Epmc, doi: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. Molecular & cellular proteomics : MCP. 2021 Jan;20:100088.

Published In

Molecular & cellular proteomics : MCP

DOI

EISSN

1535-9484

ISSN

1535-9476

Publication Date

January 2021

Volume

20

Start / End Page

100088

Related Subject Headings

  • Symporters
  • Retinal Photoreceptor Cell Outer Segment
  • Monocarboxylic Acid Transporters
  • Mice, Inbred C57BL
  • Mice
  • Membrane Proteins
  • Cell Membrane
  • Cattle
  • Biochemistry & Molecular Biology
  • Animals