Tyrosine Phosphorylation of the α Subunit of Transducin and Its Association with Src in Photoreceptor Rod Outer Segments

@article{Bell2000TyrosinePO,
  title={Tyrosine Phosphorylation of the $\alpha$ Subunit of Transducin and Its Association with Src in Photoreceptor Rod Outer Segments},
  author={M W Bell and Nirav Desai and Xiaofeng Guo and Abboud J. Ghalayini},
  journal={Journal of Neurochemistry},
  year={2000},
  volume={75}
}
Abstract: Recent evidence indicates that tyrosine phosphorylation may play important roles in retinal photoreceptor rod outer segments (ROS). We investigated the tyrosine phosphorylation of endogenous proteins in isolated bovine ROS. Several proteins with apparent molecular masses of 31, 39, 60, 83, 90, 97, 120, 140, and 180 kDa were tyrosine‐phosphorylated in ROS incubated with Mg2+, ATP, and orthovanadate. Several tyrosine kinase inhibitors significantly inhibited tyrosine phosphorylation of… 
Purification of a Src family tyrosine protein kinase from bovine retinas
  • D. Perdomo, J. Bubis
  • Medicine, Chemistry
    Zeitschrift fur Naturforschung. C, Journal of biosciences
  • 2020
TLDR
It was demonstrated that Src family tyrosine kinases were present in the cytosolic fraction of extracted bovine retinas, and it was shown that this retinal SRC family member was not capable of using transducin as a substrate.
Phosphorylation of RGS9-1 by an Endogenous Protein Kinase in Rod Outer Segments*
TLDR
RGS9-1 is phosphorylated on Ser475 in vivo, and the phosphorylation level is regulated by light and by [Ca2+], suggesting the importance of the modification in light adaptation.
Light-dependent Association of Src with Photoreceptor Rod Outer Segment Membrane Proteinsin Vivo *
TLDR
The data strongly suggest that light exposure in vivo activates Src and promotes its association through its SH2 domain with a complex containing bleached rhodopsin and arrestin either directly or indirectly.
Interaction of the insulin receptor beta-subunit with phosphatidylinositol 3-kinase in bovine ROS.
TLDR
Tyrosine phosphorylation of the beta-subunit of the insulin receptor is involved in the regulation of PI3K activity in ROS.
Light regulation of the insulin receptor in the retina
TLDR
The results suggest that light induces tyrosine phosphorylation of IRβ in outersegment membranes, which leads to the binding of p85 through its N-terminal SH2 domain and the generation of PI-3,4,5-P3.
G-protein-coupled Receptor Rhodopsin Regulates the Phosphorylation of Retinal Insulin Receptor*
TLDR
This study provides evidence for the existence of a light-mediated IR pathway in the retina that is different from the known insulin-mediated pathway in nonneuronal tissues and suggests that IR phosphorylation in rod photoreceptors is signaled through the G-protein-coupled receptor rhodopsin.
Signal Activation and Inactivation by the Gα Helical Domain: A Long-Neglected Partner in G Protein Signaling
TLDR
Emerging evidence reveals that the helical domain is an active participant in G protein signaling, which appear to underlie signal initiation by their cognate GPCRs.
Rhodopsin-regulated Insulin Receptor Signaling Pathway in Rod Photoreceptor Neurons
TLDR
Recent studies that link the photoactivation of rhodopsin to tyrosine phosphorylation of the IR and subsequent activation of phosphoinositide 3-kinase, a neuron survival factor, suggest that the physiological role of this process is to provide neuroprotection of the retina against light damage by activating proteins that protect against stress-induced apoptosis.
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TLDR
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TLDR
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