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Sci. STKE, 27 March 2001
Vol. 2001, Issue 75, p. tw3
[DOI: 10.1126/stke.2001.75.tw3]

EDITORS' CHOICE

METHODOLOGY Following Protein Activation in Real Time

Abstract:

Fluorescence resonance energy transfer (FRET) is emerging as a powerful tool that allows real-time monitoring of protein interactions in living cells. Janetopoulos et al. added fluorescent tags to the G{alpha}2 and Gß subunits of heterotrimeric guanine nucleotide binding proteins (G proteins) in Dictyostelium discoideum. The G protein-coupled receptors are a very large family of proteins that mediate the action of hormones, neurotransmitters, and other signaling molecules. In this case, the authors treated cells with a chemoattractant and then observed the dissociation of the active G protein subunits by FRET. During continuous stimulation, the physiological response to the chemoattractant subsided, but the G protein remained activated (as measured by dissociation of the heterotrimer). The authors suggest that signal adaptation must occur downstream of the activated G protein. The method is expected to be extensible to mammalian cells and should enable substantial improvement in our quantitative understanding of mechanisms of G protein signaling.

C. Janetopoulos, T. Jin, P. Devreotes, Receptor-mediated activation of heterotrimeric G-proteins in living cells. Science 291, 2408-2411 (2001). [Abstract] [Full Text]

Citation: Following Protein Activation in Real Time. Sci. STKE 2001, tw3 (2001).

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Science Signaling. ISSN 1937-9145 (pre-2008: Science's STKE. ISSN 1525-8882)