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Modulation of retinal transducin and phosphodiesterase activities by synthetic peptides of the phosphodiesterase γ‐subunit
Author(s) -
Morrison Daniel F.,
Rider Maureen A.,
Takemoto Dolores J.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80383-6
Subject(s) - transducin , phosphodiesterase , gamma subunit , cyclic guanosine monophosphate , gtpase , guanosine , pde10a , protein subunit , biochemistry , g protein , chemistry , retinal , biology , microbiology and biotechnology , biophysics , rhodopsin , enzyme , endocrinology , signal transduction , nitric oxide , gene
Synthetic peptides corresponding to various regions of the light‐activated guanosine 3′,5′‐cyclic monophosphate phosphodiesterase (PDE) γ‐subunit (PDEγ) from bovine retinal rod outer segments were synthesized and tested for their ability to inhibit PDE activity, and GTPase activity of transducin. One of these peptides, corresponding to PDEγ residues 31–45, inhibited PDE activity and GTPase activity in a dose‐dependent manner. The GTPase activity was inhibited by PDEγ‐3 non‐competitively. This region of the PDEγ subunit may be involved in the direct interaction of transducin and PDEαβ with PDEγ.