Phosphorylation of bovine rod photoreceptor cyclic GMP phosphodiesterase.

Phosphorylation of bovine rod photoreceptor cyclic GMP phosphodiesterase.
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牛视杆光感受器环 GMP 磷酸二酯酶的磷酸化。

DOI:
10.1042/bj2950049
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发表时间:
1993
期刊:
The Biochemical journal
影响因子:
--
通讯作者:
Takemoto,DJ
Takemoto,DJ
中科院分区:
--
文献类型:
--
作者:
Udovichenko,IP;Cunnick,J;Gonzales,K;Takemoto,DJ

文献摘要

被引文献

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视网膜视杆细胞的环GMP磷酸二酯酶(PDE)在光转导中起关键作用,并且由两个催化亚基(PDE α和PDE β)和两个相同的抑制亚基(PDE γ)组成。在这里,我们报告说,PDE α和PDE γ磷酸化的蛋白激酶(S)C(PKC)从大脑和杆外节(ROS)。这两种相同类型的PKC也磷酸化胰蛋白酶激活的PDE中的PDE α(没有PDE γ)。相比之下,环AMP依赖性蛋白激酶催化亚基磷酸化PDE α和PDE β,但不磷酸化PDE γ。该激酶不磷酸化胰蛋白酶激活的PDE。合成肽AKVISNLLGPREAAV(PDE α 30-44)和KQRQTRQFKSKPPKK(PDE γ 31-45)通过来自ROS的PKC抑制PDE的磷酸化。这些数据表明,PKC对PDE磷酸化的位点(每个亚基至少一个)位于PDE α和PDE γ的相应区域。针对蛋白激酶C的α、β、γ、δ、β和ζ同种型特有的肽的同工酶特异性PKC抗体用于显示ROS中PKC的主要形式是PKC α。然而,其他次要形式也存在。
The cyclic GMP phosphodiesterase (PDE) of retinal rods plays a key role in phototransduction and consists of two catalytic subunits (PDE alpha and PDE beta) and two identical inhibitory subunits (PDE gamma). Here we report that PDE alpha and PDE gamma are phosphorylated by protein kinase(s) C (PKC) from brain and rod outer segments (ROS). These same two types of PKC also phosphorylate PDE alpha in trypsin-activated PDE (without PDE gamma). In contrast, cyclic-AMP-dependent protein kinase catalytic subunit phosphorylates both PDE alpha and PDE beta, but not PDE gamma. This kinase does not phosphorylate trypsin-activated PDE. The synthetic peptides AKVISNLLGPREAAV (PDE alpha 30-44) and KQRQTRQFKSKPPKK (PDE gamma 31-45) inhibited phosphorylation of PDE by PKC from ROS. These data suggest that sites (at least one for each subunit) for phosphorylation of PDE by PKC are localized in these corresponding regions of PDE alpha and PDE gamma. Isoenzyme-specific PKC antibodies against peptides unique to the alpha, beta, gamma, delta, epsilon and zeta isoforms of protein kinase C were used to show that a major form of PKC in ROS is PKC alpha. However, other minor forms were also present.