Abstract
The polyhedral surface lattice of coated vesicles consists of three-legged hexameric protein complexes called triskelions which constitute the basic assembly unit1. The triskelion is a molecular complex of molecular weight 630,000 (Mr 630K) composed of three clathrin heavy chains (subunit 180K) and three light chains (subunits 33K and 36K) (refs 2,3). The presence of additional coated vesicle-specific proteins in the 100–130K and 50–55K range have been reported4–6. We previously described the presence of a cyclic nucleotide- and Ca2+-independent protein kinase activity in coated vesicles7 which was confirmed by others8,9. This protein kinase specifically phosphorylates the 50K protein (pp50). In this report, we show that the coated vesicle kinase and its 50K protein substrate are part of a stable multimolecular system. In addition we show that the clathrin–light chain complex stimulates the pp50 phosphorylation and only light chains are implicated in this stimulation and that the pp50 phosphorylation does not seem to be affected by the vesicle.
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Pauloin, A., Jollès, P. Internal control of the coated vesicle pp50-specific kinase complex. Nature 311, 265–267 (1984). https://doi.org/10.1038/311265a0
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DOI: https://doi.org/10.1038/311265a0
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