May 2006
Volume 47, Issue 13
Free
ARVO Annual Meeting Abstract  |   May 2006
Light–Dependent Trafficking of Growth Factor Receptor–Bound Protein 14 Requires the Photobleaching of Rhodopsin but Not Transducin Signaling
Author Affiliations & Notes
  • R.V. Rajala
    Univ of Oklahoma Hlth Sci Ctr, Oklahoma City, OK
    Ophthal/Dean McGee Eye Inst,
  • M. Tanito
    Univ of Oklahoma Hlth Sci Ctr, Oklahoma City, OK
    Ophthal/Dean McGee Eye Inst,
  • J.–X. Ma
    Univ of Oklahoma Hlth Sci Ctr, Oklahoma City, OK
    Cell Biology,
  • J. Lem
    Ophthalmology, Tufts–New England Medical Center, Boston, MA
  • A. Rajala
    Univ of Oklahoma Hlth Sci Ctr, Oklahoma City, OK
    Ophthal/Dean McGee Eye Inst,
  • Footnotes
    Commercial Relationships  R.V. Rajala, None; M. Tanito, None; J. Ma, None; J. Lem, None; A. Rajala, None.
  • Footnotes
    Support  EY00871, EY04149, EY12190, RR17703, and Research to Prevent Blindness, Inc.
Investigative Ophthalmology & Visual Science May 2006, Vol.47, 1092. doi:
  • Views
  • Share
  • Tools
    • Alerts
      ×
      This feature is available to authenticated users only.
      Sign In or Create an Account ×
    • Get Citation

      R.V. Rajala, M. Tanito, J.–X. Ma, J. Lem, A. Rajala; Light–Dependent Trafficking of Growth Factor Receptor–Bound Protein 14 Requires the Photobleaching of Rhodopsin but Not Transducin Signaling . Invest. Ophthalmol. Vis. Sci. 2006;47(13):1092.

      Download citation file:


      © ARVO (1962-2015); The Authors (2016-present)

      ×
  • Supplements
Abstract

Purpose: : We previously demonstrated light–induced tyrosine phosphorylation of the retinal insulin receptor (IR), independent of insulin secretion, and localized the light effect to photoreceptor neurons. These results suggest that there exists a cross talk between phototransduction and other signal transduction pathways. This cross talk phenomenon has been shown in other G–protein–coupled receptors (GPCRs) as many tyrosine kinase cascades are regulated by GPCRs. These studies suggest that rhodopsin might also initiate other signaling pathways. The idea that rhodopsin can initiate non–canonical signaling pathways is further supported by studies on the translocation of visual arrestin.

Methods: : We used yeast two–hybrid assay of protein–protein interaction to identify binding partners to the IR from a bovine retinal cDNA library. Rod outer segments (ROS) were prepared from the light– and dark–adapted wild type, Talpha, and Rpe65 knockout mice. Immunohistochemistry was performed on light– and dark–adapted mouse retina sections.

Results: : Yeast two–hybrid screening identified growth factor receptor–bound protein 14 (Grb14) as an IR binding partner. Grb14 is an inhibitor of protein tyrosine phosphatase 1b, which specifically dephosphorylates the IR. We found more Grb14 bound to light–adapted ROS membranes than to dark–adapted membranes. Immunohistochemical studies indicate that Grb14 is localized in the inner segment in the dark and in ROS in the light. In Talpha knockout mice, Grb14 trafficking to ROS is similar to wild–type, whereas in Rpe65 knockout mice we observed only ∼10% of Grb14 bound to both light– and dark–adapted ROS. These results suggest that rhodopsin photobleaching is required for Grb14 trafficking and proper localization to ROS, but transducin signaling is not.

Conclusions: : These studies show that rhodopsin can initiate signaling pathways other than visual transduction, and support our hypothesis that signaling proteins not directly involved in phototransduction could undergo subcellular redistribution upon illumination.

Keywords: signal transduction • photoreceptors • receptors 
×
×

This PDF is available to Subscribers Only

Sign in or purchase a subscription to access this content. ×

You must be signed into an individual account to use this feature.

×