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Related Experiment Videos

Phosducin induces a structural change in transducin beta gamma

A Loew1, Y K Ho, T Blundell

  • 1Department of Biochemistry and Molecular Biology, University of Illinois at Chicago, IL 60612-7334, USA.

Structure (London, England : 1993)
|September 18, 1998
PubMed
Summary

Phosducin binding to Gt beta gamma subunits changes their conformation, sequestering them from membranes and inhibiting G protein signaling. This structural switch regulates signal transduction cascades.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Phosducin binds Gt beta gamma subunits of transducin, inhibiting the G-protein cycle.
  • Phosducin-like proteins regulate diverse heterotrimeric G-protein signaling pathways.

Purpose of the Study:

  • To elucidate the structural mechanism by which phosducin regulates Gt beta gamma subunits.

Main Methods:

  • X-ray crystallography of a bovine retinal phosducin-Gt beta gamma complex at 2.8 A resolution.

Main Results:

  • The crystal structure reveals phosducin domains covering Gt beta gamma, inducing a conformational change.
  • A cavity forms between beta-propeller blades 6 and 7 of Gt beta gamma, accommodating the gamma subunit's farnesyl moiety.

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Conclusions:

  • Gt beta gamma subunits exist in relaxed (R) and tense (T) states, regulated by phosducin.
  • Phosducin binding induces the T state, burying the farnesyl group, sequestering Gt beta gamma to the cytosol, and inhibiting signal transduction.
  • This phosducin-mediated switch may be a general mechanism for attenuating G protein-coupled signaling.