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Related Experiment Videos

Dependence of RGS9-1 membrane attachment on its C-terminal tail.

W He1, T J Melia, C W Cowan

  • 1Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030, USA.

The Journal of Biological Chemistry
|October 26, 2001
PubMed
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Regulator of G protein signaling 9-1 (RGS9-1) is crucial for photoreceptor light response recovery. Its C-terminal domain, not G beta(5L), mediates tight binding to disc membranes.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Vision Science

Background:

  • Regulator of G protein signaling 9-1 (RGS9-1) is essential for rapid recovery of the light response in vertebrate rod and cone photoreceptors.
  • RGS9-1, a GTPase-accelerating protein (GAP), is a peripheral membrane protein of disc membranes but attaches more tightly than other phototransduction proteins.
  • The mechanism of RGS9-1 membrane attachment is unknown, as it lacks lipid modifications found on interacting proteins.

Purpose of the Study:

  • To investigate the mechanism of RGS9-1 membrane attachment.
  • To identify the specific domains or subunits responsible for RGS9-1's tight membrane binding.

Main Methods:

  • Limited proteolysis to generate RGS9-1 fragments.
  • Immunoblotting to characterize protein fragments.

Related Experiment Videos

  • Construction and testing of recombinant RGS9-1 fragments with and without the C-terminal domain and G beta(5L) subunit.
  • Treatment with urea to assess membrane-bound RGS9-1 solubility.

    • Main Results:

    • Limited proteolysis yielded a soluble RGS9-1 fragment lacking a 3-kDa C-terminal piece.
    • RGS9-1 fragments lacking the C-terminal domain exhibited significantly reduced membrane binding affinity.
    • Removal of G beta(5L) from membrane-bound RGS9-1 did not affect its tight membrane association.
    • Recombinant RGS9-1 was soluble in urea only when membranes were absent.

    Conclusions:

    • The C-terminal domain of RGS9-1 is critical for its strong binding to photoreceptor disc membranes.
    • The partner subunit G beta(5L) does not play a significant role in RGS9-1's membrane attachment.
    • RGS9-1's tight membrane binding is an intrinsic property mediated by its C-terminal domain.