Effect of the ILE86TER mutation in the Î³ subunit of cGMP phosphodiesterase (PDE6) on rod photoreceptor signaling

Article ID	Journal	Published Year	Pages	File Type
10816474	Cellular Signalling	2012	8 Pages	PDF

Abstract

âº We made PDE6 ILE86TER mice lacking the two C-terminal PDE6Î³ Ile86 and Ile87 residues. âº This mutation in vitro reduces the efficiency of PDE6Î³ inhibition of PDE6Î± and PDE6Î². âº Light responses of ILE86TER rods decayed more slowly than those of WT rods. âº Experiments with IBMX showed that mutant rods had more spontaneous PDE6 activity. âº The C-terminus of PDE6Î³ plays an essential role in control of PDE6 activity in vivo.

Keywords

PBS GTPase accelerating protein IDV cGMP phosphodiesterase Transducin PDE6 ROD PDE cGMP GTP IBMX BSA bovine serum albumin Tα Transduction isobutylmethylxanthine outer segment GDP Embryonic stem cell Retina GAP Photoreceptor Phosphodiesterase Phosphate-buffered saline cyclic guanosine monophosphate wild-type polymerase chain reaction PCR G-protein Vision Guanosine triphosphate guanosine diphosphate

Related Topics

Life Sciences Biochemistry, Genetics and Molecular Biology Biochemistry

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Effect of the ILE86TER mutation in the Î³ subunit of cGMP phosphodiesterase (PDE6) on rod photoreceptor signaling

Authors

Stephen H. Tsang, Michael L. Woodruff, Chyuan-Sheng Lin, Barry D. Jacobson, Matthew C. Naumann, Chun Wei Hsu, Richard J. Davis, Marianne C. Cilluffo, Jeannie Chen, Gordon L. Fain,