The ER (endoplasmic reticulum) is a major protein folding and modification organelle. In its lumen, the ER processes a third of all newly synthesized proteins. To accomplish this task, numerous resident proteins capture the nascent and newly synthesized proteins. The underlying luminal protein–protein interactions, however, are inherently difficult to analyse, mainly due to their transient nature and the rather specialized environment of the ER. To overcome these limitations, we developed a PCA (protein fragment complementation assay) based on the citrine variant of YFP (yellow fluorescent protein). YFP PCA was successfully applied to visualize the protein interactions of the cargo transport receptor ERGIC-53 (endoplasmic reticulum–Golgi intermediate compartment protein of 53 kDa) with its luminal interaction partner MCFD2 (multiple coagulation factor deficiency protein 2) and its cargo proteins cathepsin Z and cathepsin C in a specific manner. With the prospect of screening cDNA libraries for novel protein–protein interactions, YFP PCA is a promising emerging technique for mapping protein interactions inside the secretory pathway in a genome-wide setting.
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November 2007
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Conference Article|
October 25 2007
Visualization of protein interactions inside the secretory pathway
B. Nyfeler;
B. Nyfeler
1Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland
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H.-P. Hauri
H.-P. Hauri
1
1Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland
1To whom correspondence should be addressed (email Hans-Peter.Hauri@unibas.ch).
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Publisher: Portland Press Ltd
Received:
June 13 2007
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2007 Biochemical Society
2007
Biochem Soc Trans (2007) 35 (5): 970–973.
Article history
Received:
June 13 2007
Citation
B. Nyfeler, H.-P. Hauri; Visualization of protein interactions inside the secretory pathway. Biochem Soc Trans 1 November 2007; 35 (5): 970–973. doi: https://doi.org/10.1042/BST0350970
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