Kinetic Scaffolding Mediated by a Phospholipase C–β and G q Signaling Complex-Reference-Cited by-同舟云学术

Kinetic Scaffolding Mediated by a Phospholipase C–β and G q Signaling Complex

Published:2010-11-12 Issue:6006 Volume:330 Page:974-980
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Waldo Gary L.¹,Ricks Tiffany K.¹,Hicks Stephanie N.¹,Cheever Matthew L.¹,Kawano Takeharu²,Tsuboi Kazuhito²,Wang Xiaoyue³,Montell Craig³,Kozasa Tohru²⁴,Sondek John¹⁵⁶,Harden T. Kendall¹⁶

Affiliation:

1. Department of Pharmacology, University of North Carolina School of Medicine, Chapel Hill, NC 27599, USA.

2. Department of Pharmacology, University of Illinois, Chicago, IL 60612, USA.

3. Departments of Biological Chemistry and Neuroscience, Center for Sensory Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.

4. Laboratory for Systems Biology and Medicine, Research Center for Advanced Science and Technology, University of Tokyo, Tokyo 153-8904, Japan.

5. Department of Biochemistry, University of North Carolina School of Medicine, Chapel Hill, NC 27599, USA.

6. Lineberger Cancer Center, University of North Carolina School of Medicine, Chapel Hill, NC 27599, USA.

Abstract

Reciprocal Regulation An essential step in many signaling cascades is inositol lipid hydrolysis catalyzed by phospholipase C–β. The latter is activated by the α subunit of the heterotrimeric G protein Gq, and it in turn inactivates Gαq, thus sharpening the signal. Waldo et al. (p. 974 , published online 21 October) report structural and biochemical data that explain the basis of this reciprocal regulation. One domain of phospholipase C–β binds to activated Gαq. Though the phospholipase C–β active site remains occluded in the structure, the plug is probably removed upon G protein–dependent orientation of the lipase at the membrane. A second domain of phospholipase C–β accelerates guanosine triphosphate hydrolysis by Gαq causing the signaling complex to dissociate.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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