Intracellular transport of a heterologous membrane protein,the human transferrin receptor,in<Emphasis Type="Italic"> Saccharomyces cerevisiae</Emphasis> |
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Authors: | Bianka?Prinz Ulf?Stahl Email author" target="_blank">Christine?LangEmail author |
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Institution: | (1) Institute for Biotechnology, Department of Microbiology and Genetics, Berlin University of Technology, Gustav-Meyer-Allee 25, 13355, Berlin, Germany, |
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Abstract: | We have analyzed the intracellular behavior of the human transferrin receptor (TfR) in Saccharomyces cerevisiae. The major part of the heterologously expressed TfR, which has previously been used as a model for heterologous expression
of membrane proteins in yeast, is localized in the endoplasmic reticulum (ER) membranes; a minor fraction is present in the
plasma membrane (PM). The stability of the TfR depends on vacuolar proteases, implying that it is degraded in the vacuolar
compartment. Degradation is further dependent on favorable transport conditions to this compartment. The main bottleneck of
transport seems to be the transition from the ER to the PM. The chaperone Cne1p, which is involved in quality control in the
ER, plays a role in regulating the amount of heterologous TfR, as deletion of CNE1 leads to significant accumulation of the protein. This is the first demonstration of the involvement of CNE1 in regulating the level of heterologous membrane proteins.
Electronic Publication |
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Keywords: | Intracellular transport Heterologous membrane protein Yeast CNE1 Transferrin receptor |
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