cGMP suppresses GTPase activity of a portion of transducin equimolar to phosphodiesterase in frog rod outer segments. Light-induced cGMP decreases as a putative feedback mechanism of the photoresponse.
Open Access
- 1 October 1991
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 266 (28) , 18530-18537
- https://doi.org/10.1016/s0021-9258(18)55094-8
Abstract
No abstract availableKeywords
This publication has 72 references indexed in Scilit:
- Subunit stoichiometry of retinal rod cGMP phosphodiesteraseBiochemistry, 1990
- Transducin GTPase provides for rapid quenching of the cGMP cascade in rod outer segmentsFEBS Letters, 1989
- Sub‐second turnover of transducin GTPase in bovine rod outer segments A light scattering studyFEBS Letters, 1988
- On the role of transducin GTPase in the quenching of a phosphodiesterase cascade of visionFEBS Letters, 1987
- Detection of Ca2+-dependent cyclic GMP binding protein in frog rod outer segmentsFEBS Letters, 1987
- Retinal rod GTPase turnover rate increases with concentration: A key to the control of visual excitation?Biochemical and Biophysical Research Communications, 1987
- Guanylate cyclase in rod outer segments of the toad retinaFEBS Letters, 1986
- Light-suppressible, cyclic GMP-sensitive conductance in the plasma membrane of a truncated rod outer segmentNature, 1985
- The effect of rhodopsin phosphorylation on the light‐dependent activation of phosphodiesterase from bovine rod outer segmentsFEBS Letters, 1985
- Ca2+-dependent changes in cyclic GMP levels are not correlated with opening and closing of the light-dependent permeability of toad photoreceptors.The Journal of general physiology, 1982