ArticleCellular and molecular life sciences : CMLS2010
Discrimination between alternate membrane protein topologies in living cells using GFP/YFP tagging and pH exchange.
Article in Cellular and molecular life sciences : CMLS, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Non-invasive tools for analysis of plasma membrane protein topology in living cells.Methods (San Diego, Calif.) · 2025Article
- Enquiry into the Topology of Plasma Membrane-Localized PIN Auxin Transport Components.Molecular plant · 2016Article
- Visualization of phosphatidic acid fluctuations in the plasma membrane of living cells.PloS one · 2014Article
- Failure of prion protein oxidative folding guides the formation of toxic transmembrane forms.The Journal of biological chemistry · 2012Article
- A never ending race for new and improved fluorescent proteins.BMC biology · 2012Article
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Authors and funding
7 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Membrane protein function is determined by the relative organization of the protein domains with respect to the membrane. We have experimentally verified the topology of a protein with diverse orientations arising from a single primary sequence (the cellular prion protein, PrP(C)), a novel somatostatin truncated receptor, and the Golgi-associated protein GPBP(91). Tagging with fluorescent proteins (FP) allows location of their expression at the plasma membrane or at endomembranes, but does not inform about their orientation. Exploiting the pH dependency of some FPs, we developed a pH exchange assay in which extracellularly exposed FPs are quenched by application of low pH buffer. We constructed standards to demonstrate and calibrate the assay, and the method was adapted for acidic organelle membrane proteins. This method can serve as a proof of concept, experimentally confirming and/or discriminating in living cells among theoretical topology predictions, providing the proportion of inside/outside orientation for proteins with multiple forms.
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