Use of G-protein fusions to monitor integral membrane protein-protein interactions in yeast - PubMed (original) (raw)

. 2000 Oct;18(10):1075-9.

doi: 10.1038/80274.

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

K N Ehrhard et al. Nat Biotechnol. 2000 Oct.

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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 gamma-subunit. If the binding partners interact, G-protein signaling is disrupted. We demonstrate interaction between known binding partners, syntaxin 1a 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.

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