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First published online April 23, 2008

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Longer and stronger with Cav1

Caveolin-1 (Cav1) organizes into plasma membrane domains that are known as caveolae and which are involved in the localization of signalling proteins. Some cell lines are known to have caveolae, whereas others do not, and it is unclear why this is the case. On page 1363, Suzanne Scarlata and colleagues use two rat cell types (one that lacks Cav1 and one that forms caveolae-like domains) to investigate whether Cav1 affects Ca²⁺ signalling through the Gβ-PLCβ signalling system. The authors monitor the interaction of G_q and Gβ in the cell types using FRET to observe the association of proteins on membrane surfaces of living cells in real time, and FCS to measure the average mobility of cell surface proteins. They find that, in the resting state, Gβ and G_q are similarly associated but, following activation, Cav1 seems to increase the separation between the two subunits and binds preferentially to G_q. Interactions between G_q and Gβ subunits, which are required for signal termination, appear to be hindered by this binding. This prolongs the activated state, and the authors observe a corresponding increased and sustained Ca²⁺ signal. Therefore, Cav1 might have a role in determining the duration of G-protein signals.

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Related articles in JCS:

Caveolin-1 alters Ca²⁺ signal duration through specific interaction with the G_q family of G proteins

Parijat Sengupta, Finly Philip, and Suzanne Scarlata
JCS 2008 121: 1363-1372. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?