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TitleBestrophin-2 and glutamine synthetase form a complex for glutamate release.
Journal, issue, pagesNature, Vol. 611, Issue 7934, Page 180-187, Year 2022
Publish dateOct 26, 2022
AuthorsAaron P Owji / Kuai Yu / Alec Kittredge / Jiali Wang / Yu Zhang / Tingting Yang /
PubMed AbstractBestrophin-2 (BEST2) is a member of the bestrophin family of calcium-activated anion channels that has a critical role in ocular physiology. Here we uncover a directional permeability of BEST2 to ...Bestrophin-2 (BEST2) is a member of the bestrophin family of calcium-activated anion channels that has a critical role in ocular physiology. Here we uncover a directional permeability of BEST2 to glutamate that heavily favours glutamate exit, identify glutamine synthetase (GS) as a binding partner of BEST2 in the ciliary body of the eye, and solve the structure of the BEST2-GS complex. BEST2 reduces cytosolic GS activity by tethering GS to the cell membrane. GS extends the ion conducting pathway of BEST2 through its central cavity and inhibits BEST2 channel function in the absence of intracellular glutamate, but sensitizes BEST2 to intracellular glutamate, which promotes the opening of BEST2 and thus relieves the inhibitory effect of GS. We demonstrate the physiological role of BEST2 in conducting chloride and glutamate and the influence of GS in non-pigmented ciliary epithelial cells. Together, our results reveal a novel mechanism of glutamate release through BEST2-GS.
External linksNature / PubMed:36289327 / PubMed Central
MethodsEM (single particle)
Resolution2.0 Å
Structure data

28025

8ecy

EMDB-28025, PDB-8ecy:
cryoEM structure of bovine bestrophin-2 and glutamine synthetase complex
Method: EM (single particle) / Resolution: 2.0 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-CL:
Unknown entry / Chloride

ChemComp-MN:
Unknown entry

ChemComp-HOH:
WATER / Water

Source
  • Homo sapiens (human)
  • bos taurus (cattle)
KeywordsMEMBRANE PROTEIN / ion channel / transport / anion channel

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