Oligomeric state of purified transient receptor potential melastatin-1 (TRPM1), a protein essential for dim light vision.

ABSTRACT: Transient receptor potential melastatin-1 (TRPM1) is essential for the light-induced depolarization of retinal ON bipolar cells. TRPM1 likely forms a multimeric channel complex, although almost nothing is known about the structure or subunit composition of channels formed by TRPM1 or any of its close relatives. Recombinant TRPM1 was robustly expressed in insect cells, but only a small fraction was localized to the plasma membrane. Similar intracellular localization was observed when TRPM1 was heterologously expressed in mammalian cells. TRPM1 was affinity-purified from Sf9 cells and complexed with amphipol, followed by detergent removal. In blue native gels and size exclusion chromatography, TRPM1 migrated with a mobility consistent with detergent- or amphipol-bound dimers. Cross-linking e

SUBMITTER: Agosto MA 

PROVIDER: S-EPMC4175340 | biostudies-literature | 2014 Sep

REPOSITORIES: biostudies-literature