spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

First published online August 9, 2007
doi: 10.1242/10.1242/jcs.001404

Journal of Cell Science 120, 2953-2962 (2007)
Published by The Company of Biologists 2007
This Article
Right arrow Figures Only
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplementary Material
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Abankwa, D.
Right arrow Articles by Vogel, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Abankwa, D.
Right arrow Articles by Vogel, H.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

Research Article

A FRET map of membrane anchors suggests distinct microdomains of heterotrimeric G proteins

Daniel Abankwa* and Horst Vogel

Ecole Polytechnique Fédérale de Lausanne (EPFL), Institut des Sciences et Ingénierie Chimiques, CH-1015 Lausanne, Switzerland

e-mails: d.abankwa{at}imb.uq.edu.au; horst.vogel{at}epfl.ch

Accepted 21 June 2007

The standard model of heterotrimeric G protein signaling postulates a dissociation of G{alpha} and Gbeta{gamma} subunits after activation. We hypothesized that the different combination of lipid-modifications on G{alpha} and G{alpha}beta{gamma} subunits directs them into different microdomains. By characterizing rapidly and at high sensitivity 38 fluorescence resonance energy transfer (FRET) pairs of heterotrimeric-G-protein constructs, we defined their microdomains in relation to each other, free from the constraints of the raft/non-raft dualism. We estimated that in a cell ~30% of these membrane-anchored proteins are mostly clustered in 3400-16,200 copies of 30-nm microdomains. We found that the membrane anchors of G{alpha} and G{alpha}beta{gamma} subunits of both the Gi/o and Gq family co-cluster differently with microdomain markers. Moreover, anchors of the G{alpha}i/o and G{alpha}q subunits co-clustered only weakly, whereas constructs that contained the anchors of the corresponding heterotrimers co-clustered considerably, suggesting the existence of at least three types of microdomain. Finally, FRET experiments with full-length heterotrimeric G proteins confirmed that the inactive, heterotrimerized G{alpha} subunit is in microdomains shared by heterotrimers from different subclasses, from where it displaces upon activation into a membrane-anchor- and subclass-specific microdomain.

Key words: FRET, Heterotrimeric G protein, Microdomain, Nanodomain, Raft


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?


This article has been cited by other articles:


Home page
 Mol. Pharmacol.Home page
L. Milan-Lobo, I. Gsandtner, E. Gaubitzer, D. Runzler, F. Buchmayer, G. Kohler, A. Bonci, M. Freissmuth, and H. H. Sitte
Subtype-Specific Differences in Corticotropin-Releasing Factor Receptor Complexes Detected by Fluorescence Spectroscopy
Mol. Pharmacol., December 1, 2009; 76(6): 1196 - 1210.
[Abstract] [Full Text] [PDF]


© The Company of Biologists Ltd 2007