Oct 11, 2012

Phosphorylation of mouse melanopsin by protein kinase A

PloS One
Joseph R BlasicPhyllis R Robinson

Abstract

The visual pigment melanopsin is expressed in intrinsically photosensitive retinal ganglion cells (ipRGCs) in the mammalian retina, where it is involved in non-image forming light responses including circadian photoentrainment, pupil constriction, suppression of pineal melatonin synthesis, and direct photic regulation of sleep. It has recently been shown that the melanopsin-based light response in ipRGCs is attenuated by the neurotransmitter dopamine. Here, we use a heterologous expression system to demonstrate that mouse melanopsin can be phosphorylated by protein kinase A, and that phosphorylation can inhibit melanopsin signaling in HEK cells. Site-directed mutagenesis experiments revealed that this inhibitory effect is primarily mediated by phosphorylation of sites T186 and S287 located in the second and third intracellular loops of melanopsin, respectively. Furthermore, we show that this phosphorylation can occur in vivo using an in situ proximity-dependent ligation assay (PLA). Based on these data, we suggest that the attenuation of the melanopsin-based light response by dopamine is mediated by direct PKA phosphorylation of melanopsin, rather than phosphorylation of a downstream component of the signaling cascade.

  • References29
  • Citations11

References

  • References29
  • Citations11

Citations

Mentioned in this Paper

Vertebrates
Biochemical Pathway
Calcium [EPC]
Polymerase
Transfection
Phosphoserine
HEK293 Cells
Signaling Cascade
Carboxy-Terminal Amino Acid
Entire Retina

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