Light‐dependent in vivo phosphorylation of an inhibitory subunit of cGMP‐phosphodiesterase in frog rod photoreceptor outer segments

FEBS Letters

Hayashi, Fumio¹ 

[1]Department of Biology, Faculty of Science, Kobe University, Nada, Kobe 657, Japan

关键词: Photoreceptor;    Rod outer segments;    Phosphorylation;    cGMP-phosphodiesterase;    Inhibitory subunit;    Protein phosphatase;    PDE;    phosphodiesterase;    Pα;    Pβ and Pγ;    α;    β and γ subunits of phosphodiesterase;    ROS;    rod outer segments;    Tα;    Tβ and Tγ;    α;    β and γ subunits of transducin;    GTP;    guanosine 5'-triphosphate;    ATP;    adenosine 5'-triphosphate;    NEPHGE;    non-equilibrium pH gel electrophoresis;    SDS;    sodium dodedcyl sulfate;   

DOI  :  10.1016/0014-5793(94)80365-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In vivo phosphorylation of P_γ, an inhibitory subunit of cGMP-phosphodiesterase of frog (Rana catesbeiana) photoreceptor rod outer segments, was investigated using a quick-freezing technique and a newly developed method for the preparation of rod outer segments. Light-dependent phosphorylation of P_γ was observed. Okadaic acid, a potent inhibitor of protein phosphatases 1 and 2A, enhanced the apparent incorporation of ³²P into P_γ suggesting that P_γ is in equilibrium between phosphorylation and dephosphorylation. Neither phorbol ester, a potent activator of protein kinase C, nor changes in the extracellular Ca²⁺ concentration affected the in vivo phosphorylation of P_γ.

【 授权许可】

Unknown