Open AccessSupramolecular organization of rhodopsin in rod photoreceptor cell membranes
Author(s) -
Paul S.H. Park
Publication year - 2021
Publication title -
pflügers archiv für die gesamte physiologie des menschen und der tiere/pflügers archiv
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.428
H-Index - 129
eISSN - 0365-267X
pISSN - 0031-6768
DOI - 10.1007/s00424-021-02522-5
Subject(s) - rhodopsin , scotopic vision , supramolecular chemistry , membrane , opsin , biophysics , biology , microbiology and biotechnology , neuroscience , chemistry , crystallography , retina , retinal , biochemistry , crystal structure
Rhodopsin is the light receptor in rod photoreceptor cells that initiates scotopic vision. Studies on the light receptor span well over a century, yet questions about the organization of rhodopsin within the photoreceptor cell membrane still persist and a consensus view on the topic is still elusive. Rhodopsin has been intensely studied for quite some time, and there is a wealth of information to draw from to formulate an organizational picture of the receptor in native membranes. Early experimental evidence in apparent support for a monomeric arrangement of rhodopsin in rod photoreceptor cell membranes is contrasted and reconciled with more recent visual evidence in support of a supramolecular organization of rhodopsin. What is known so far about the determinants of forming a supramolecular structure and possible functional roles for such an organization are also discussed. Many details are still missing on the structural and functional properties of the supramolecular organization of rhodopsin in rod photoreceptor cell membranes. The emerging picture presented here can serve as a springboard towards a more in-depth understanding of the topic.