Light-Induced Tyrosine Phosphorylation of Rod Outer Segment Membrane Proteins Regulate the Translocation, Membrane Binding and Activation of Type II α Phosphatidylinositol-5-Phosphate 4-Kinase

@article{Huang2010LightInducedTP,
  title={Light-Induced Tyrosine Phosphorylation of Rod Outer Segment Membrane Proteins Regulate the Translocation, Membrane Binding and Activation of Type II α Phosphatidylinositol-5-Phosphate 4-Kinase},
  author={Zhong Huang and Robert E. Anderson and Wei Cao and Allan F. Wiechmann and Raju V. S. Rajala},
  journal={Neurochemical Research},
  year={2010},
  volume={36},
  pages={627-635}
}
Type II phosphatidylinositol 5-phosphate 4-kinase (PIPKIIα) catalyzes the synthesis of phosphatidylinositol-4,5-bisphosphate (PI-4,5-P2), an essential lipid second messenger that may be involved in the regulation of phototransduction, neuroprotection, and morphogenesis in the vertebrate retina. Here we report that in rodent and transgenic frogs, the light-mediated activity and membrane binding of PIPKIIα in rod outer segments (ROS) is dependent on tyrosine phosphorylation of ROS proteins. The… CONTINUE READING