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Volume 271, Number 51, Issue of December 20, 1996 pp. 33123-33130
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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The Light Chain Subunit Is Required for Clathrin Function in Saccharomyces cerevisiae

(Received for publication, May 30, 1996, and in revised form, September 20, 1996)

From the Molecular Biology Institute and the Department of Biological Chemistry, University of California, Los Angeles, California 90095-1737

Clathrin, a multimeric protein involved in intracellular protein trafficking, is composed of three heavy chains (Chc) and three light chains (Clc). Upon disruption (clc1) of the single Clc-encoding gene (CLC1) in yeast, the steady state protein levels of Chc decreased 5-10-fold compared with wild type cells; consequently, phenotypes exhibited by clc1 cells may result indirectly from the loss of Chc as opposed to the absence of Clc. As an approach to directly examine Clc function, clc1 strains were generated that carry a multicopy plasmid containing the clathrin heavy chain gene (CHC1), resulting in levels of Chc 5-10-fold elevated over wild-type levels. As with deletion of CHC1, deletion of CLC1 results in defects in growth, receptor-mediated endocytosis, and maturation of the mating pheromone -factor. However, elevated Chc expression in clc1 cells partially suppresses the growth and -factor maturation defects displayed by clc1 cells alone. Biochemical analyses indicate that trimerization and assembly of Chc are perturbed in the absence of Clc, resulting in vesiculation defects. Our results demonstrate that the light chain subunit of clathrin is required for efficient Chc trimerization, proper formation of clathrin coats, and the generation of clathrin-coated vesicles.

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