Mechanistic Basis for G Protein Function in ON Bipolar Cells View Full Text


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Chapter Info

DATE

2014-09-05

AUTHORS

Noga Vardi , Anuradha Dhingra

ABSTRACT

The synapse from photoreceptors to ON bipolar cells is unique among feedforward synapses in that it inverts the sign of the light response from hyperpolarizing in photoreceptors to depolarizing in ON bipolar cells. This occurs due to a highly specialized cascade that uses the metabotropic glutamate receptor mGluR6 to activate the heterotrimeric G protein Go, which then closes the nonselective cation channel TRPM1. When glutamate in the synaptic cleft drops, Go is deactivated rapidly and TRPM1 opens; this deactivation is key to the rising phase of the light response. This chapter presents the evidence that established Gαo, Gβ3, and Gγ13 as Go’s subunits in ON bipolar cells. While Go’s key function is to couple mGluR6 with an effector, the different subunits also contribute to maintaining the synaptic integrity, at both the molecular and structural levels. Evidence suggests that Go’s deactivation is accelerated by at least two different types of guanosine triphosphatase (GTPase) activating protein (GAP) complexes: RGS11/Gβ5/R9AP and RGS7/Gβ5/GPR179. A third complex may contain RGS11/Gβ5/GPR179. Certain elements of these GAP complexes (RGS7 and RGS11) are redundant, but others (Gβ5 and GPR179) are crucial. Different molecules likely modulate the cascade, but so far only one, Ret-PCP2, was clearly shown to accelerate the light response in rod bipolar and certain types of ON cone bipolar cells. Interestingly, most cascade elements including mGluR6 and the GAPs are restricted to the dendritic tips, but the G protein subunits Ret-PCP2 and TRPM1 are also present in other parts of the cell. More... »

PAGES

81-97

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4939-1218-6_6

DOI

http://dx.doi.org/10.1007/978-1-4939-1218-6_6

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1032526431


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