The Binding Properties and Physiological Functions of Recoverin
- 1Institute of Molecular Life Sciences, University of Zurich, Switzerland
Recoverin (Rcv) is a low molecular-weight, neuronal calcium sensor primarily located in photoreceptor outer segments of the vertebrate retina. Ca2+-bound Rcv has been proposed to inhibit G-protein-coupled receptor kinase (GRK) in darkness. During the light response, the Ca2+-free Rcv releases GRK, which in turn phosphorylates visual pigment, ultimately leading to the cessation of the visual transduction cascade.
Technological advances over the last decade have contributed significantly to a deeper understanding of Rcv function. These include both biophysical and biochemical approaches that will be discussed in this review article.
Furthermore, electrophysiological experiments uncovered addition functions of Rcv, such as regulation of the lifetime of Phosphodiesterase-Transducin complex. Recently, attention has been drawn to different roles in rod and cone photoreceptors.
This review focuses on Rcv binding properties to Ca2+, disc membrane and GRK, and its physiological functions in phototransduction decay and during light adaptation.
Keywords: Recoverin, Phototransduction cascade, G protein-coupled receptor kinase, Visual pigment phosphorylation, Ca2+ myristoyl switch
Received: 31 Aug 2018;
Accepted: 04 Dec 2018.
Edited by:Karl-Wilhelm Koch, University of Oldenburg, Germany
Reviewed by:Ching-Kang J. Chen, Baylor College of Medicine, United States
Lorenzo Cangiano, University of Pisa, Italy
Copyright: © 2018 ZANG and Neuhauss. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
* Correspondence: Prof. Stephan C. Neuhauss, University of Zurich, Institute of Molecular Life Sciences, Zürich, Switzerland, firstname.lastname@example.org