May 2008
Volume 49, Issue 13
Free
ARVO Annual Meeting Abstract  |   May 2008
RGS6 Binding Partners in Mouse Retina
Author Affiliations & Notes
  • E. Posokhova
    Pharmacology, University of Minnesota, Minneapolis, Minnesota
  • K. Martemyanov
    Pharmacology, University of Minnesota, Minneapolis, Minnesota
  • Footnotes
    Commercial Relationships  E. Posokhova, None; K. Martemyanov, None.
  • Footnotes
    Support  NIH Grant EY018139
Investigative Ophthalmology & Visual Science May 2008, Vol.49, 774. doi:https://doi.org/
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    • Get Citation

      E. Posokhova, K. Martemyanov; RGS6 Binding Partners in Mouse Retina. Invest. Ophthalmol. Vis. Sci. 2008;49(13):774. doi: https://doi.org/.

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

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Abstract

Purpose: : G proteins are known to be major players in visual signal transduction. In the retina, G protein signaling is critically shaped by the R7 group of Regulator of G Protein Signaling (R7 RGS) family. Currently, molecular context of R7 RGS protein function is understood only for RGS9, a key regulator of photoreceptor signaling. Other R7 RGS proteins are abundant in the inner retina where they are thought to regulate G protein signal transduction cascades downstream from the photoreceptors. In the efforts to understand the molecular composition of such pathways we conducted a search for the interaction partners of an R7 RGS member, RGS6.

Methods: : Immunoprecipitation with anti RGS6 antibodies was used for isolation of RGS6-containing complexes. Eluates were resolved by gel electrophoresis. Coomasie-stained bands were excised, digested with trypsin and subjected to mass-spectrometric identification by MALDI TOF spectrometry. Data was analyzed using ProteinPilot software.

Results: : Analysis of proteins eluted from antibodies indicated a presence of several unique bands which were not found in the control immunoprecipitation experiment with retinas lacking RGS6. Retinal RGS6 was present as a single major species of approximately 54kDa. The most prominent co-precipitating protein was identified as short splice isoform of Gbeta5. Additionally, several novel interactions were found.

Conclusions: : RGS6 in the retina exists as a macromolecular complex involving short splice isoform of Gbeta5.

Keywords: retina • proteomics • signal transduction 
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