The calcium-binding site of clathrin light chains

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

    Research output: Contribution to journalArticle

    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

    Fingerprint

    Clathrin Light Chains
    Clathrin
    Binding Sites
    Calcium
    Light
    Clathrin-Coated Vesicles
    EF Hand Motifs
    Calcium-Binding Proteins
    Calmodulin
    Yeast
    Yeasts

    Cite this

    Näthke, I., Hill, B. L., Parham, P., & Brodsky, F. M. (1990). The calcium-binding site of clathrin light chains. Journal of Biological Chemistry, 265(30), 18621-18627.
    Näthke, I. ; Hill, B. L. ; Parham, P. ; Brodsky, F. M. / The calcium-binding site of clathrin light chains. In: Journal of Biological Chemistry. 1990 ; Vol. 265, No. 30. pp. 18621-18627.
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    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.",
    author = "I. N{\"a}thke and Hill, {B. L.} and P. Parham and Brodsky, {F. M.}",
    year = "1990",
    language = "English",
    volume = "265",
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    Näthke, I, Hill, BL, Parham, P & Brodsky, FM 1990, 'The calcium-binding site of clathrin light chains', Journal of Biological Chemistry, vol. 265, no. 30, pp. 18621-18627.

    The calcium-binding site of clathrin light chains. / Näthke, I.; Hill, B. L.; Parham, P.; Brodsky, F. M.

    In: Journal of Biological Chemistry, Vol. 265, No. 30, 1990, p. 18621-18627.

    Research output: Contribution to journalArticle

    TY - JOUR

    T1 - The calcium-binding site of clathrin light chains

    AU - Näthke, I.

    AU - Hill, B. L.

    AU - Parham, P.

    AU - Brodsky, F. M.

    PY - 1990

    Y1 - 1990

    N2 - 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.

    AB - 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.

    M3 - Article

    VL - 265

    SP - 18621

    EP - 18627

    JO - Journal of Biological Chemistry

    JF - Journal of Biological Chemistry

    SN - 0021-9258

    IS - 30

    ER -

    Näthke I, Hill BL, Parham P, Brodsky FM. The calcium-binding site of clathrin light chains. Journal of Biological Chemistry. 1990;265(30):18621-18627.