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A genetic system based on split-ubiquitin for the analysis of interactions between membrane proteins in vivo

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Stagljar, Igor, Korostensky, Chantal, Johnsson, Nils, te Heesen, Stephan·1998·Proceedings of the National Academy of Sciences

Abstract

A detection system for interactions between membrane proteins in vivo is described. The system is based on split-ubiquitin [Johnsson, N. & Varshavsky, A. (1994) Proc. Natl. Acad. Sci. USA 91, 10340–10344]. Interaction between two membrane proteins is detected by proteolytic cleavage of a protein fusion. The cleavage releases a transcription factor, which activates reporter genes in the nucleus. As a result, interaction between membrane proteins can be analyzed by the means of a colorimetric assay. We use membrane proteins of the endoplasmic reticulum as a model system. Wbp1p and Ost1p are both subunits of the oligosaccharyl transferase membrane protein complex. The Alg5 protein also localizes to the membrane of the endoplasmic reticulum, but does not interact with the oligosaccharyltransferase. Specific interactions are detected between Wbp1p and Ost1p, but not between Wbp1p and Alg5p. The new system might be useful as a genetic and biochemical tool for the analysis of interactions between membrane proteins in vivo .

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Metadata

Authors
Stagljar, I., Korostensky, C., Johnsson, N., & te Heesen, S.
Venue
Proceedings of the National Academy of Sciences
Published
1998-04-28
Volume
95
Issue
9
Pages
5187-5192
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2096211374
Cited by
596
References
0
FWCI
3.49
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: A genetic system based on split-ubiquitin for the analysis of interactions between membrane proteins in vivo. https://app.cochat.ai/papers/10.1073/pnas.95.9.5187
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Stagljar, I., Korostensky, C., Johnsson, N., & te Heesen, S. (1998). A genetic system based on split-ubiquitin for the analysis of interactions between membrane proteins in vivo. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.95.9.5187

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