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J Biol Chem

Title:		The light chain subunit is required for clathrin function in Saccharomyces cerevisiae
Author(s):		Chu DS; Pishvaee B; Payne GS;
Address:		"Molecular Biology Institute and the Department of Biological Chemistry, University of California, Los Angeles, California 90095-1737, USA"
Journal Title:		J Biol Chem
Year:		1996
Volume:		271
Issue:		51
Page Number:		33123 - 33130
DOI:		10.1074/jbc.271.51.33123
ISSN/ISBN:		0021-9258 (Print) 0021-9258 (Linking)
Abstract:		"Clathrin, a multimeric protein involved in intracellular protein trafficking, is composed of three heavy chains (Chc) and three light chains (Clc). Upon disruption (clc1Delta) 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 clc1Delta cells may result indirectly from the loss of Chc as opposed to the absence of Clc. As an approach to directly examine Clc function, clc1Delta 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 alpha-factor. However, elevated Chc expression in clc1Delta cells partially suppresses the growth and alpha-factor maturation defects displayed by clc1Delta 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"
Keywords:		Biological Transport Cell Compartmentation Cell Membrane/metabolism Clathrin/*physiology Coated Vesicles/*metabolism/ultrastructure Endocytosis Fungal Proteins/metabolism Intracellular Membranes/metabolism Macromolecular Substances Mating Factor Mutagenes;
Notes:		"MedlineChu, D S Pishvaee, B Payne, G S eng GM 07185/GM/NIGMS NIH HHS/ GM39040/GM/NIGMS NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. 1996/12/20 J Biol Chem. 1996 Dec 20; 271(51):33123-30. doi: 10.1074/jbc.271.51.33123"