RapamycinFungusV1, Main, Exploration, bibRecord, 001059

Detection and characterization of protein interactions in vivo by a simple live-cell imaging method.

Identifieur interne : 001059 ( Main/Exploration ); précédent : 001058; suivant : 001060

Detection and characterization of protein interactions in vivo by a simple live-cell imaging method.

Auteurs : Oriol Gallego [Espagne] ; Tanja Specht ; Thorsten Brach ; Arun Kumar ; Anne-Claude Gavin ; Marko Kaksonen

Source :

PloS one [ 1932-6203 ] ; 2013.

RBID : pubmed:23658712

Descripteurs français

English descriptors

Abstract

Over the last decades there has been an explosion of new methodologies to study protein complexes. However, most of the approaches currently used are based on in vitro assays (e.g. nuclear magnetic resonance, X-ray, electron microscopy, isothermal titration calorimetry etc). The accurate measurement of parameters that define protein complexes in a physiological context has been largely limited due to technical constrains. Here, we present PICT (Protein interactions from Imaging of Complexes after Translocation), a new method that provides a simple fluorescence microscopy readout for the study of protein complexes in living cells. We take advantage of the inducible dimerization of FK506-binding protein (FKBP) and FKBP-rapamycin binding (FRB) domain to translocate protein assemblies to membrane associated anchoring platforms in yeast. In this assay, GFP-tagged prey proteins interacting with the FRB-tagged bait will co-translocate to the FKBP-tagged anchor sites upon addition of rapamycin. The interactions are thus encoded into localization changes and can be detected by fluorescence live-cell imaging under different physiological conditions or upon perturbations. PICT can be automated for high-throughput studies and can be used to quantify dissociation rates of protein complexes in vivo. In this work we have used PICT to analyze protein-protein interactions from three biological pathways in the yeast Saccharomyces cerevisiae: Mitogen-activated protein kinase cascade (Ste5-Ste11-Ste50), exocytosis (exocyst complex) and endocytosis (Ede1-Syp1).

DOI: 10.1371/journal.pone.0062195
PubMed: 23658712
PubMed Central: PMC3641059

Affiliations:

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<front><div type="abstract" xml:lang="en">Over the last decades there has been an explosion of new methodologies to study protein complexes. However, most of the approaches currently used are based on in vitro assays (e.g. nuclear magnetic resonance, X-ray, electron microscopy, isothermal titration calorimetry etc). The accurate measurement of parameters that define protein complexes in a physiological context has been largely limited due to technical constrains. Here, we present PICT (Protein interactions from Imaging of Complexes after Translocation), a new method that provides a simple fluorescence microscopy readout for the study of protein complexes in living cells. We take advantage of the inducible dimerization of FK506-binding protein (FKBP) and FKBP-rapamycin binding (FRB) domain to translocate protein assemblies to membrane associated anchoring platforms in yeast. In this assay, GFP-tagged prey proteins interacting with the FRB-tagged bait will co-translocate to the FKBP-tagged anchor sites upon addition of rapamycin. The interactions are thus encoded into localization changes and can be detected by fluorescence live-cell imaging under different physiological conditions or upon perturbations. PICT can be automated for high-throughput studies and can be used to quantify dissociation rates of protein complexes in vivo. In this work we have used PICT to analyze protein-protein interactions from three biological pathways in the yeast Saccharomyces cerevisiae: Mitogen-activated protein kinase cascade (Ste5-Ste11-Ste50), exocytosis (exocyst complex) and endocytosis (Ede1-Syp1).</div>
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<tree><noCountry><name sortKey="Brach, Thorsten" sort="Brach, Thorsten" uniqKey="Brach T" first="Thorsten" last="Brach">Thorsten Brach</name>
<name sortKey="Gavin, Anne Claude" sort="Gavin, Anne Claude" uniqKey="Gavin A" first="Anne-Claude" last="Gavin">Anne-Claude Gavin</name>
<name sortKey="Kaksonen, Marko" sort="Kaksonen, Marko" uniqKey="Kaksonen M" first="Marko" last="Kaksonen">Marko Kaksonen</name>
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	Serveur d'exploration sur la rapamycine et les champignons
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Serveur d'exploration sur la rapamycine et les champignons

Detection and characterization of protein interactions in vivo by a simple live-cell imaging method.

Detection and characterization of protein interactions in vivo by a simple live-cell imaging method.

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