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Membrane attachment is key to protecting transducin GTPase-activating complex from intracellular proteolysis in photoreceptors.

Publication ,  Journal Article
Gospe, SM; Baker, SA; Kessler, C; Brucato, MF; Winter, JR; Burns, ME; Arshavsky, VY
Published in: The Journal of neuroscience : the official journal of the Society for Neuroscience
October 2011

The members of the R7 regulator of G-protein signaling (RGS) protein subfamily are versatile regulators of G-protein signaling throughout the nervous system. Recent studies indicate that they are often found in complexes with membrane anchor proteins that serve as versatile modulators of their activity, intracellular targeting, and stability. One striking example is the interplay between the membrane anchor R9AP and the RGS9-1 · Gβ5 GTPase-activating complex responsible for the rapid inactivation of the G-protein transducin in vertebrate photoreceptor cells during their recovery from light excitation. The amount of this complex in photoreceptors sets their temporal resolution and is precisely regulated by the expression level of R9AP, which serves to protect the RGS9-1 and Gβ5 subunits from intracellular proteolysis. In this study, we investigated the mechanism by which R9AP performs its protective function in mouse rods and found that it is entirely confined to recruiting RGS9-1 · Gβ5 to cellular membranes. Furthermore, membrane attachment of RGS9-1 · Gβ5 is sufficient for its stable expression in rods even in the absence of R9AP. Our second finding is that RGS9-1 · Gβ5 possesses targeting information that specifies its exclusion from the outer segment and that this information is neutralized by association with R9AP to allow outer segment targeting. Finally, we demonstrate that the ability of R9AP · RGS9-1 · Gβ5 to accelerate GTP hydrolysis on transducin is independent of its means of membrane attachment, since replacing the transmembrane domain of R9AP with a site for lipid modification did not impair the catalytic activity of this complex.

Duke Scholars

Published In

The Journal of neuroscience : the official journal of the Society for Neuroscience

DOI

EISSN

1529-2401

ISSN

0270-6474

Publication Date

October 2011

Volume

31

Issue

41

Start / End Page

14660 / 14668

Related Subject Headings

  • Signal Transduction
  • SNARE Proteins
  • Retina
  • RGS Proteins
  • Proteolysis
  • Photoreceptor Cells, Vertebrate
  • Neurology & Neurosurgery
  • Mutation
  • Mice, Transgenic
  • Mice, Inbred C57BL
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Gospe, S. M., Baker, S. A., Kessler, C., Brucato, M. F., Winter, J. R., Burns, M. E., & Arshavsky, V. Y. (2011). Membrane attachment is key to protecting transducin GTPase-activating complex from intracellular proteolysis in photoreceptors. The Journal of Neuroscience : The Official Journal of the Society for Neuroscience, 31(41), 14660–14668. https://doi.org/10.1523/jneurosci.3516-11.2011
Gospe, Sidney M., Sheila A. Baker, Christopher Kessler, Martha F. Brucato, Joan R. Winter, Marie E. Burns, and Vadim Y. Arshavsky. “Membrane attachment is key to protecting transducin GTPase-activating complex from intracellular proteolysis in photoreceptors.The Journal of Neuroscience : The Official Journal of the Society for Neuroscience 31, no. 41 (October 2011): 14660–68. https://doi.org/10.1523/jneurosci.3516-11.2011.
Gospe SM, Baker SA, Kessler C, Brucato MF, Winter JR, Burns ME, et al. Membrane attachment is key to protecting transducin GTPase-activating complex from intracellular proteolysis in photoreceptors. The Journal of neuroscience : the official journal of the Society for Neuroscience. 2011 Oct;31(41):14660–8.
Gospe, Sidney M., et al. “Membrane attachment is key to protecting transducin GTPase-activating complex from intracellular proteolysis in photoreceptors.The Journal of Neuroscience : The Official Journal of the Society for Neuroscience, vol. 31, no. 41, Oct. 2011, pp. 14660–68. Epmc, doi:10.1523/jneurosci.3516-11.2011.
Gospe SM, Baker SA, Kessler C, Brucato MF, Winter JR, Burns ME, Arshavsky VY. Membrane attachment is key to protecting transducin GTPase-activating complex from intracellular proteolysis in photoreceptors. The Journal of neuroscience : the official journal of the Society for Neuroscience. 2011 Oct;31(41):14660–14668.

Published In

The Journal of neuroscience : the official journal of the Society for Neuroscience

DOI

EISSN

1529-2401

ISSN

0270-6474

Publication Date

October 2011

Volume

31

Issue

41

Start / End Page

14660 / 14668

Related Subject Headings

  • Signal Transduction
  • SNARE Proteins
  • Retina
  • RGS Proteins
  • Proteolysis
  • Photoreceptor Cells, Vertebrate
  • Neurology & Neurosurgery
  • Mutation
  • Mice, Transgenic
  • Mice, Inbred C57BL