The TRPM1 channel in ON-bipolar cells is gated by both the α and the βγ subunits of the G-protein Go View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2016-02-17

AUTHORS

Ying Xu, Cesare Orlandi, Yan Cao, Shengyan Yang, Chan-Il Choi, Vijayakanth Pagadala, Lutz Birnbaumer, Kirill A. Martemyanov, Noga Vardi

ABSTRACT

Transmission from photoreceptors to ON bipolar cells in mammalian retina is mediated by a sign-inverting cascade. Upon binding glutamate, the metabotropic glutamate receptor mGluR6 activates the heterotrimeric G-protein Gαoβ3γ13 and this leads to closure of the TRPM1 channel (melastatin). TRPM1 is thought to be constitutively open, but the mechanism that leads to its closure is unclear. We investigated this question in mouse rod bipolar cells by dialyzing reagents that modify the activity of either Gαo or Gβγ and then observing their effects on the basal holding current. After opening the TRPM1 channels with light, a constitutively active mutant of Gαo closed the channel, but wild-type Gαo did not. After closing the channels by dark adaptation, phosducin or inactive Gαo (both sequester Gβγ) opened the channel while the active mutant of Gαo did not. Co-immunoprecipitation showed that TRPM1 interacts with Gβ3 and with the active and inactive forms of Gαo. Furthermore, bioluminescent energy transfer assays indicated that while Gαo interacts with both the N- and the C- termini of TRPM1, Gβγ interacts only with the N-terminus. Our physiological and biochemical results suggest that both Gαo and Gβγ bind TRPM1 channels and cooperate to close them. More... »

PAGES

20940

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/srep20940

DOI

http://dx.doi.org/10.1038/srep20940

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1016200549

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/26883481


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