The Protein Journal

, 28:362 | Cite as

Hydrophobic Interactions Stabilize the Basigin-MCT1 Complex

  • NiCole A. Finch
  • Paul J. Linser
  • Judith D. OchrietorEmail author


Previous reports demonstrated that monocarboxylate transporter-1 (MCT1) interacts with Basigin. It was hypothesized that the two proteins interact via the transmembrane domain of Basigin, specifically through the glutamate residue within the domain. We therefore sought to test this hypothesis and determine which amino acids of the Basigin protein are necessary for the interaction with MCT1. Probes consisting of the full-length putative transmembrane domain, as well as small regions of the domain, were generated for use in ELISA binding assays using endogenous mouse MCT1. Site directed mutagenesis of candidate residues was performed and probes were generated for ELISA analyses to determine the specific residues involved. The data suggest that hydrophobic residues at the N- and C-termini of the putative transmembrane domain of Basigin interact with MCT1, but the glutamate plays no role. The previously proposed hypothesis is partially correct, in that the putative transmembrane domain of Basigin does interact with MCT1.


Basigin Monocarboxylate transporter 1 Metabolism Retina ELISA 



Alkaline phosphatase


Bovine serum albumin


Cluster of differentiation


Complementary deoxyribonucleic acid


Enzyme-linked immunosorbant assay


Extracellular matrix metalloproteinase inducer


Fluorescence resonance energy transfer




Isopropyl β-d-thiogalactopyranoside


Monocarboxylate transporter


Phosphate buffered saline


Polymerase chain reaction


Retinal pigmented epithelium


Transmembrane domain


Six C-terminal histidines



This work was supported by NIH F32EY13918 and UNF Academic Affairs (to JDO) and NSF IBN-0113697 (to PJL). We thank Dr. Andrea Kohn, University of Florida Whitney Laboratory for Marine Biosciences and Dr. Michael Lentz, University of North Florida for constructive criticisms. We also thank Mr. Greggory Wilhoite, Ms. Bahishta Yaqubi, and Mr. Anthony Vinson for technical assistance.


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Copyright information

© Springer Science+Business Media, LLC 2009

Authors and Affiliations

  • NiCole A. Finch
    • 1
  • Paul J. Linser
    • 2
  • Judith D. Ochrietor
    • 1
    Email author
  1. 1.Department of BiologyUniversity of North FloridaJacksonvilleUSA
  2. 2.Whitney Laboratory for Marine Biosciences and the Department of Anatomy and Cell BiologyUniversity of FloridaSt. AugustineUSA

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