The calcium-binding site of clathrin light chains

I. Näthke, B. L. Hill, P. Parham, F. M. Brodsky

    Research output: Contribution to journalArticlepeer-review

    31 Citations (Scopus)

    Abstract

    Clathrin light chains are calcium-binding proteins (Mooibroek, M. J., Michiel, D. F., and Wang, J. H. (1987) J. Biol. Chem. 262, 25-28) and clathrin assembly can be modulated by calcium in vitro. Thus, intracellular calcium may play a regulatory role in the function of clathrin-coated vesicles. The structural basis for calcium's influence on clathrin-mediated processes has been defined using recombinant deletion mutants and isolated fragments of the light chains. A single calcium-binding site, formed by residues 85-96, is present in both mammalian light chains (LCa and LCb) and in the single yeast light chain. This sequence has structural similarity to the calcium-binding EF-hand loops of calmodulin and related proteins. In mammalian light chains, the calcium-binding sequence is flanked by domains that regulate clathrin assembly and disassembly.
    Original languageEnglish
    Pages (from-to)18621-18627
    Number of pages7
    JournalJournal of Biological Chemistry
    Volume265
    Issue number30
    Publication statusPublished - 1990

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