Use of G-protein fusions to monitor integral membrane protein-protein interactions in yeast

Kathleen N. Ehrhard, Jörg J. Jacoby, Xin Yuan Fu, Reinhard Jahn, Henrik G. Dohlman

Research output: Contribution to journalArticle

59 Citations (Scopus)

Abstract

The control of protein-protein interactions is a fundamental aspect of cell regulation. Here we describe a new approach to detect the interaction of two proteins in vivo. By this method, one binding partner is an integral membrane protein whereas the other is soluble but fused to a G-protein γ-subunit. If the binding partners interact, G-protein signaling is disrupted. We demonstrate interaction between known binding partners, syntaxin 1 a with neuronal Sec1 (nSec1), and the fibroblast-derived growth factor receptor 3 (FGFR3) with SNT-1. In addition, we describe a genetic screen to identify nSec1 mutants that are expressed normally, but are no longer able to bind to syntaxin 1a. This provides a convenient method to study interactions of integral membrane proteins, a class of molecules that has been difficult to study by existing biochemical or genetic methods.

Original languageEnglish (US)
Pages (from-to)1075-1079
Number of pages5
JournalNature Biotechnology
Volume18
Issue number10 SUPPL.
StatePublished - 2000
Externally publishedYes

Fingerprint

Syntaxin 1
GTP-Binding Proteins
Yeast
Membrane Proteins
Fusion reactions
Yeasts
Proteins
Membranes
Receptor, Fibroblast Growth Factor, Type 3
Growth Factor Receptors
Protein Subunits
Fibroblasts
Molecular Biology
Molecules

ASJC Scopus subject areas

  • Microbiology

Cite this

Ehrhard, K. N., Jacoby, J. J., Fu, X. Y., Jahn, R., & Dohlman, H. G. (2000). Use of G-protein fusions to monitor integral membrane protein-protein interactions in yeast. Nature Biotechnology, 18(10 SUPPL.), 1075-1079.

Use of G-protein fusions to monitor integral membrane protein-protein interactions in yeast. / Ehrhard, Kathleen N.; Jacoby, Jörg J.; Fu, Xin Yuan; Jahn, Reinhard; Dohlman, Henrik G.

In: Nature Biotechnology, Vol. 18, No. 10 SUPPL., 2000, p. 1075-1079.

Research output: Contribution to journalArticle

Ehrhard, KN, Jacoby, JJ, Fu, XY, Jahn, R & Dohlman, HG 2000, 'Use of G-protein fusions to monitor integral membrane protein-protein interactions in yeast', Nature Biotechnology, vol. 18, no. 10 SUPPL., pp. 1075-1079.
Ehrhard KN, Jacoby JJ, Fu XY, Jahn R, Dohlman HG. Use of G-protein fusions to monitor integral membrane protein-protein interactions in yeast. Nature Biotechnology. 2000;18(10 SUPPL.):1075-1079.
Ehrhard, Kathleen N. ; Jacoby, Jörg J. ; Fu, Xin Yuan ; Jahn, Reinhard ; Dohlman, Henrik G. / Use of G-protein fusions to monitor integral membrane protein-protein interactions in yeast. In: Nature Biotechnology. 2000 ; Vol. 18, No. 10 SUPPL. pp. 1075-1079.
@article{15fdb99b9cf44e92a3abe4e946c92715,
title = "Use of G-protein fusions to monitor integral membrane protein-protein interactions in yeast",
abstract = "The control of protein-protein interactions is a fundamental aspect of cell regulation. Here we describe a new approach to detect the interaction of two proteins in vivo. By this method, one binding partner is an integral membrane protein whereas the other is soluble but fused to a G-protein γ-subunit. If the binding partners interact, G-protein signaling is disrupted. We demonstrate interaction between known binding partners, syntaxin 1 a with neuronal Sec1 (nSec1), and the fibroblast-derived growth factor receptor 3 (FGFR3) with SNT-1. In addition, we describe a genetic screen to identify nSec1 mutants that are expressed normally, but are no longer able to bind to syntaxin 1a. This provides a convenient method to study interactions of integral membrane proteins, a class of molecules that has been difficult to study by existing biochemical or genetic methods.",
author = "Ehrhard, {Kathleen N.} and Jacoby, {J{\"o}rg J.} and Fu, {Xin Yuan} and Reinhard Jahn and Dohlman, {Henrik G.}",
year = "2000",
language = "English (US)",
volume = "18",
pages = "1075--1079",
journal = "Nature Biotechnology",
issn = "1087-0156",
publisher = "Nature Publishing Group",
number = "10 SUPPL.",

}

TY - JOUR

T1 - Use of G-protein fusions to monitor integral membrane protein-protein interactions in yeast

AU - Ehrhard, Kathleen N.

AU - Jacoby, Jörg J.

AU - Fu, Xin Yuan

AU - Jahn, Reinhard

AU - Dohlman, Henrik G.

PY - 2000

Y1 - 2000

N2 - The control of protein-protein interactions is a fundamental aspect of cell regulation. Here we describe a new approach to detect the interaction of two proteins in vivo. By this method, one binding partner is an integral membrane protein whereas the other is soluble but fused to a G-protein γ-subunit. If the binding partners interact, G-protein signaling is disrupted. We demonstrate interaction between known binding partners, syntaxin 1 a with neuronal Sec1 (nSec1), and the fibroblast-derived growth factor receptor 3 (FGFR3) with SNT-1. In addition, we describe a genetic screen to identify nSec1 mutants that are expressed normally, but are no longer able to bind to syntaxin 1a. This provides a convenient method to study interactions of integral membrane proteins, a class of molecules that has been difficult to study by existing biochemical or genetic methods.

AB - The control of protein-protein interactions is a fundamental aspect of cell regulation. Here we describe a new approach to detect the interaction of two proteins in vivo. By this method, one binding partner is an integral membrane protein whereas the other is soluble but fused to a G-protein γ-subunit. If the binding partners interact, G-protein signaling is disrupted. We demonstrate interaction between known binding partners, syntaxin 1 a with neuronal Sec1 (nSec1), and the fibroblast-derived growth factor receptor 3 (FGFR3) with SNT-1. In addition, we describe a genetic screen to identify nSec1 mutants that are expressed normally, but are no longer able to bind to syntaxin 1a. This provides a convenient method to study interactions of integral membrane proteins, a class of molecules that has been difficult to study by existing biochemical or genetic methods.

UR - http://www.scopus.com/inward/record.url?scp=0033776891&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033776891&partnerID=8YFLogxK

M3 - Article

VL - 18

SP - 1075

EP - 1079

JO - Nature Biotechnology

JF - Nature Biotechnology

SN - 1087-0156

IS - 10 SUPPL.

ER -