M-Track: detecting short-lived protein-protein interactions in vivo

Aurora Zuzuarregui Miro; Thomas Kupka; Bhumika Bhatt; Ilse Dohnal; Ingrid Mudrak; Christina Friedmann; Stefan Schüchner; Ingrid Frohner; Gustav Ammerer; Egon Ogris

M-Track: detecting short-lived protein-protein interactions in vivo

Aurora Zuzuarregui Miro, Thomas Kupka, Bhumika Bhatt, Ilse Dohnal, Ingrid Mudrak, Christina Friedmann, Stefan Schüchner, Ingrid Frohner, Gustav Ammerer, Egon Ogris

Department of Biochemistry and Cell Biology

Publications: Contribution to journal › Article › Peer Reviewed

Abstract

We developed a protein-proximity assay in yeast based on fusing a histone lysine methyltransferase onto a bait and its substrate onto a prey. Upon binding, the prey is stably methylated and detected by methylation-specific antibodies. We applied this approach to detect varying interaction affinities among proteins in a mitogen-activated protein kinase pathway and to detect short-lived interactions between protein phosphatase 2A and its substrates that have so far escaped direct detection.

Original language	English
Pages (from-to)	594-596
Number of pages	3
Journal	Nature Methods
Volume	9
Publication status	Published - 2012

Austrian Fields of Science 2012

106002 Biochemistry

Cite this

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title = "M-Track: detecting short-lived protein-protein interactions in vivo",

abstract = "We developed a protein-proximity assay in yeast based on fusing a histone lysine methyltransferase onto a bait and its substrate onto a prey. Upon binding, the prey is stably methylated and detected by methylation-specific antibodies. We applied this approach to detect varying interaction affinities among proteins in a mitogen-activated protein kinase pathway and to detect short-lived interactions between protein phosphatase 2A and its substrates that have so far escaped direct detection.",

author = "{Zuzuarregui Miro}, Aurora and Thomas Kupka and Bhumika Bhatt and Ilse Dohnal and Ingrid Mudrak and Christina Friedmann and Stefan Sch{\"u}chner and Ingrid Frohner and Gustav Ammerer and Egon Ogris",

note = "doi: 10.1038/nmeth.2017",

year = "2012",

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volume = "9",

pages = "594--596",

journal = "Nature Methods",

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TY - JOUR

T1 - M-Track: detecting short-lived protein-protein interactions in vivo

AU - Zuzuarregui Miro, Aurora

AU - Kupka, Thomas

AU - Bhatt, Bhumika

AU - Dohnal, Ilse

AU - Mudrak, Ingrid

AU - Friedmann, Christina

AU - Schüchner, Stefan

AU - Frohner, Ingrid

AU - Ammerer, Gustav

AU - Ogris, Egon

N1 - doi: 10.1038/nmeth.2017

PY - 2012

Y1 - 2012

N2 - We developed a protein-proximity assay in yeast based on fusing a histone lysine methyltransferase onto a bait and its substrate onto a prey. Upon binding, the prey is stably methylated and detected by methylation-specific antibodies. We applied this approach to detect varying interaction affinities among proteins in a mitogen-activated protein kinase pathway and to detect short-lived interactions between protein phosphatase 2A and its substrates that have so far escaped direct detection.

AB - We developed a protein-proximity assay in yeast based on fusing a histone lysine methyltransferase onto a bait and its substrate onto a prey. Upon binding, the prey is stably methylated and detected by methylation-specific antibodies. We applied this approach to detect varying interaction affinities among proteins in a mitogen-activated protein kinase pathway and to detect short-lived interactions between protein phosphatase 2A and its substrates that have so far escaped direct detection.

M3 - Article

SN - 1548-7091

VL - 9

SP - 594

EP - 596

JO - Nature Methods

JF - Nature Methods

ER -

M-Track: detecting short-lived protein-protein interactions in vivo

Abstract

Austrian Fields of Science 2012

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