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Calmodulin affinity for brain coated vesicle proteins.

N Moskowitz, W Schook, M Lisanti

    Journal of Neurochemistry
    |June 1, 1982
    PubMed
    Summary
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    This study characterizes calmodulin

    Area of Science:

    • Cell Biology
    • Neuroscience
    • Biochemistry

    Background:

    • Calmodulin is a key calcium-binding protein involved in cellular signaling.
    • Coated vesicles are essential for intracellular trafficking.

    Purpose of the Study:

    • To systematically characterize the affinity of calmodulin for brain coated vesicles.
    • To identify calmodulin-binding proteins within coated vesicles.

    Main Methods:

    • 125I-labeled calmodulin binding assays.
    • Scatchard analysis to determine binding kinetics.
    • Radioimmunoassay to quantify calmodulin in coated vesicles.
    • Affinity chromatography using Sepharose 4B-calmodulin.

    Main Results:

    Related Experiment Videos

  • Coated vesicles possess two calmodulin binding sites: one high-affinity (KD = 3.9 nM) and one low-affinity (KD = 102 nM).
  • Calmodulin is intrinsically associated with the vesicle, not the clathrin coat.
  • Proteins of Mr 100,000, 55,000, and 30,000 were identified as Ca2+-dependent calmodulin binders.
  • A 30,000 Mr protein doublet was confirmed as a calmodulin binding site.

    • Conclusions:

    • Calmodulin binds to brain coated vesicles via specific protein interactions.
    • The 100,000 and 55,000 Mr proteins are likely components of the Ca2+-Mg2+-ATPase complex.
    • Calmodulin's association with coated vesicles may regulate ATPase activity and Ca2+ transport.