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J. Cell Biol., Volume 146, Number 2, July 26, 1999 273-284
Copyright © 1999 by The Rockefeller University Press.

Expression of the 180-kD Ribosome Receptor Induces Membrane Proliferation and Increased Secretory Activity in Yeast

Frank Beckera, Laura Block-Alpera, Gerald Nakamuraa, Josephine Haradaa, K. Dane Wittrupb, and David I. Meyera
a Department of Biological Chemistry and the Molecular Biology Institute, University of California, Los Angeles School of Medicine, Los Angeles, California 90024
b Department of Chemical Engineering, University of Illinois, Urbana, Illinois 61801

Correspondence to: David I. Meyer, Department of Biological Chemistry, University of California, Los Angeles School of Medicine, Los Angeles, CA 90024-1737., dimeyer{at}ucla.edu (E-mail), (310) 206-3122 (phone), (310) 206-5197 (fax)

Expression of the canine 180-kD ribosome receptor (p180) in yeast cells resulted in a marked proliferation of intracellular membranes. The type of membranes observed varied with the expression of specific portions of p180. Rough membranes predominated when the ribosome binding domain of p180 was present, whereas expression constructs lacking this region resulted in smooth membranes. Northern analysis indicated that expression of the NH2-terminal 767 amino acids ({Delta}CT), which include the ribosome binding domain, upregulated the transcription and translation of genes involved in exocytosis. The membranes that were proliferated were functional as these cells overcame a temperature-sensitive translocation defect. Most significantly, cells that overexpressed {Delta}CT and proliferated rough endoplasmic reticulum exhibited severalfold higher levels of secretion of an ectopically expressed secretory protein. We conclude that p180 expression triggers a cascade of events leading to an increase in secretory potential akin to the terminal differentiation of mammalian secretory cells and tissues.

Key Words: secretion, endoplasmic reticulum, membrane biogenesis, yeast, ribosome receptor


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