Novel functions of clathrin light chains: Clathrin heavy chain trimerization is defective in light chain-deficient yeast

Kristen M. Huang, Lisa Gullberg, Karen K. Nelson, Christopher J. Stefan, Kendall Blumer, Sandra K. Lemmon

Research output: Contribution to journalArticle

42 Scopus citations

Abstract

Clathrin is a major coat protein involved in sorting and retention of proteins at the late Golgi and in endocytosis from the cell surface. The clathrin triskelion contains three heavy chains, which provide the structural backbone of the clathrin lattice and three light chains, which are thought to regulate the formation or disassembly of clathrin coats. To better understand the function of the clathrin light chain, we characterized yeast strains carrying a disruption of the clathrin light chain gene (CLC1). Light chain-deficient cells showed phenotypes similar to those displayed by yeast that have a disruption in the clathrin heavy chain gene (CHC1). In clc1-Δ cells, the steady state level of the clathrin heavy chain was reduced to 20%-25% of wild-type levels and most of the heavy chain was not trimerized. If CHC1 was overexpressed in clc1-Δ cells, heavy chain trimers were detected and several clc1-Δ phenotypes were partially rescued. These results indicate that the light chain is important for heavy chain trimerization and the heavy chain still has some function in the absence of the light chain. In yeast, deletion of CHC1 is lethal in strains carrying the scd1-i allele, while strains carrying the scd1-v allele can survive without the heavy chain. In previous studies we isolated several multicopy suppressors of inviability of chc1-Δ scd1-i cells. Surprisingly, one of these suppressors, SCD4, is identical to CLC1. Overexpression of CLC1 in viable chc1-Δ scd1-v strains rescued some but not all of the phenotypes displayed by these cells. In the absence of the heavy chain, the light chain was not found in a high molecular mass complex, but still associated with membranes. These results suggest that the light chain can function independently of the clathrin heavy chain in yeast.

Original languageEnglish (US)
Pages (from-to)899-910
Number of pages12
JournalJournal of Cell Science
Volume110
Issue number7
StatePublished - Apr 1 1997
Externally publishedYes

Keywords

  • Clathrin
  • Endocytosis
  • Golgi retention
  • Saccharomyces cerevisiae
  • Triskelion

ASJC Scopus subject areas

  • Cell Biology

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