Rhodopsin: the functional significance of asn-linked glycosylation and other post-translational modifications.
Rhodopsin, the G-protein coupled receptor in retinal rod photoreceptors, is a highly conserved protein that undergoes several types of post-translational modifications. These modifications are essential to maintain the protein's structure as well as its proper function in the visual transduction cycle. Rhodopsin is N-glycosylated at Asn-2 and Asn-15 in its extracellular N-terminal domain. Mutations within the glycosylation consensus sequences of rhodopsin cause autosomal dominant retinitis pigmentosa, a disease that leads to blindness. Several groups have studied the role of rhodopsin's N-linked glycan chains in protein structure and function using a variety of approaches. These include the generation of a transgenic mouse model, study of a naturally occurring mutant animal model, in vivo pharmacological inhibition of glycosylation, and in vitro analyses using transfected COS-1 cells. These studies have provided insights into the possible role of rhodopsin glycosylation, but have yielded conflicting results.
Murray
Anne R
AR
Department of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104, USA.
Fliesler
Steven J
SJ
Al-Ubaidi
Muayyad R
MR
D000595:Amino Acid Sequence; D000818:Animals; D001216:Asparagine / Q000737:chemistry*; D006031:Glycosylation; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational; D012243:Rhodopsin / Q000737:chemistry / Q000502:physiology*; D017386:Sequence Homology, Amino Acid
D001216:Asparagine; D012243:Rhodopsin