Structural biology of 11-cis-retinaldehyde production in the classical visual cycle

Author:

Daruwalla Anahita1,Choi Elliot H.1,Palczewski Krzysztof12ORCID,Kiser Philip D.123

Affiliation:

1. Department of Pharmacology, School of Medicine, Case Western Reserve University, Cleveland, OH, U.S.A.

2. Cleveland Center for Membrane and Structural Biology, Case Western Reserve University, Cleveland, OH, U.S.A.

3. Research Service, Louis Stokes Cleveland VA Medical Center, Cleveland, OH, U.S.A.

Abstract

The vitamin A derivative 11-cis-retinaldehyde plays a pivotal role in vertebrate vision by serving as the chromophore of rod and cone visual pigments. In the initial step of vision, a photon is absorbed by this chromophore resulting in its isomerization to an all-trans state and consequent activation of the visual pigment and phototransduction cascade. Spent chromophore is released from the pigments through hydrolysis. Subsequent photon detection requires the delivery of regenerated 11-cis-retinaldehyde to the visual pigment. This trans–cis conversion is achieved through a process known as the visual cycle. In this review, we will discuss the enzymes, binding proteins and transporters that enable the visual pigment renewal process with a focus on advances made during the past decade in our understanding of their structural biology.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference149 articles.

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3. Retinoid isomerase inhibitors impair but do not block mammalian cone photoreceptor function;Kiser;J. Gen. Physiol.,2018

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