Mapping Protein-Protein Interactions by Quantitative Proteomics

Research output: Contribution to journalJournal articleResearch

Abstract

Proteins exert their function inside a cell generally in multiprotein complexes. These complexes are highly dynamic structures changing their composition over time and cell state. The same protein may thereby fulfill different functions depending on its binding partners. Quantitative mass spectrometry (MS)-based proteomics in combination with affinity purification protocols has become the method of choice to map and track the dynamic changes in protein-protein interactions, including the ones occurring during cellular signaling events. Different quantitative MS strategies have been used to characterize protein interaction networks. In this chapter we describe in detail the use of stable isotope labeling by amino acids in cell culture (SILAC) for the quantitative analysis of stimulus-dependent dynamic protein interactions.
Original languageEnglish
JournalMethods in Molecular Biology
Volume658
Pages (from-to)267-278
Number of pages12
ISSN1064-3745
DOIs
Publication statusPublished - 2010

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Proteins
Isotope Labeling
Protein Interaction Maps
Amino Acids

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title = "Mapping Protein-Protein Interactions by Quantitative Proteomics",
abstract = "Proteins exert their function inside a cell generally in multiprotein complexes. These complexes are highly dynamic structures changing their composition over time and cell state. The same protein may thereby fulfill different functions depending on its binding partners. Quantitative mass spectrometry (MS)-based proteomics in combination with affinity purification protocols has become the method of choice to map and track the dynamic changes in protein-protein interactions, including the ones occurring during cellular signaling events. Different quantitative MS strategies have been used to characterize protein interaction networks. In this chapter we describe in detail the use of stable isotope labeling by amino acids in cell culture (SILAC) for the quantitative analysis of stimulus-dependent dynamic protein interactions.",
author = "Joern Dengjel and Irina Kratchmarova and Blagoy Blagoev",
year = "2010",
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pages = "267--278",
journal = "Methods in Molecular Biology",
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Mapping Protein-Protein Interactions by Quantitative Proteomics. / Dengjel, Joern; Kratchmarova, Irina; Blagoev, Blagoy.

In: Methods in Molecular Biology, Vol. 658, 2010, p. 267-278.

Research output: Contribution to journalJournal articleResearch

TY - JOUR

T1 - Mapping Protein-Protein Interactions by Quantitative Proteomics

AU - Dengjel, Joern

AU - Kratchmarova, Irina

AU - Blagoev, Blagoy

PY - 2010

Y1 - 2010

N2 - Proteins exert their function inside a cell generally in multiprotein complexes. These complexes are highly dynamic structures changing their composition over time and cell state. The same protein may thereby fulfill different functions depending on its binding partners. Quantitative mass spectrometry (MS)-based proteomics in combination with affinity purification protocols has become the method of choice to map and track the dynamic changes in protein-protein interactions, including the ones occurring during cellular signaling events. Different quantitative MS strategies have been used to characterize protein interaction networks. In this chapter we describe in detail the use of stable isotope labeling by amino acids in cell culture (SILAC) for the quantitative analysis of stimulus-dependent dynamic protein interactions.

AB - Proteins exert their function inside a cell generally in multiprotein complexes. These complexes are highly dynamic structures changing their composition over time and cell state. The same protein may thereby fulfill different functions depending on its binding partners. Quantitative mass spectrometry (MS)-based proteomics in combination with affinity purification protocols has become the method of choice to map and track the dynamic changes in protein-protein interactions, including the ones occurring during cellular signaling events. Different quantitative MS strategies have been used to characterize protein interaction networks. In this chapter we describe in detail the use of stable isotope labeling by amino acids in cell culture (SILAC) for the quantitative analysis of stimulus-dependent dynamic protein interactions.

U2 - 10.1007/978-1-60761-780-8_16

DO - 10.1007/978-1-60761-780-8_16

M3 - Journal article

VL - 658

SP - 267

EP - 278

JO - Methods in Molecular Biology

JF - Methods in Molecular Biology

SN - 1064-3745

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