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Sci Signal. 2008 Jun 24;1(25):re5. doi: 10.1126/scisignal.125re5.

Dissociation of heterotrimeric g proteins in cells.

Author information

1
Department of Pharmacology and Toxicology, Medical College of Georgia, Augusta, GA 30912-2300, USA. nlambert@mcg.edu

Erratum in

  • Sci Signal. 2008 Jul 15;1(28):er3.

Abstract

Heterotrimeric G proteins dissociate into their component Galpha and Gbetagamma subunits when these proteins are activated in solution. Until recently, it has not been known if subunit dissociation also occurs in cells. The development of optical methods to study G protein activation in live cells has made it possible to demonstrate heterotrimer dissociation at the plasma membrane. However, subunit dissociation is far from complete, and many active [guanosine triphosphate (GTP)-bound] heterotrimers are intact in a steady state. This unexpectedly reluctant dissociation calls for inclusion of a GTP-bound heterotrimeric state in models of the G protein cycle and places renewed emphasis on the relation between subunit dissociation and effector activation.

PMID:
18577758
DOI:
10.1126/scisignal.125re5
[Indexed for MEDLINE]

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