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Journal of Histochemistry and Cytochemistry, Vol. 51, 545-548, April 2003, Copyright © 2003, The Histochemical Society, Inc.

BRIEF REPORT

Localization of the BiP Molecular Chaperone with Respect to Endoplasmic Reticulum Foci Containing the Cystic Fibrosis Transmembrane Conductance Regulator in Yeast

Mara L. Sullivanb, Robert T. Youkera, Simon C. Watkinsb, and Jeffrey L. Brodskya
a Department of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania
b Center for Biological Imaging, University of Pittsburgh, Pittsburgh, Pennsylvania

Correspondence to: Jeffrey L. Brodsky, 274 Crawford Hall, Dept. of Biological Sciences, U. of Pittsburgh, Pittsburgh, PA 15260. E-mail: jbrodsky@pitt.edu

Almost all secreted proteins pass through the endoplasmic reticulum (ER), an organelle that is equipped to tolerate and/or degrade misfolded proteins. We report here that yeast expressing the cystic fibrosis transmembrane conductance regulator (CFTR) concentrate the protein at defined sites in the ER membrane that are not necessarily enriched for the ER molecular chaperone BiP. We propose that these sites are Russell bodies, an ER subcompartment in which misfolded proteins are stored and can be targeted for degradation. (J Histochem Cytochem 51:545–548, 2003)

Key Words: Russell bodies, aggresomes, ER, CFTR, BiP, chaperone, yeast, ERAD


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