In vivo phosphorylation of clathrin-coated vesicle proteins from rat reticulocytes

D. Bar-Zvi, S. T. Mosley, D. Branton

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37 Scopus citations

Abstract

We have studied the in vivo phosphorylation of clathrin-coated vesicle proteins from rat reticulocytes. The major 32P-labeled polypeptides of clathrin-coated vesicles isolated from metabolically labeled cells were the 165-, 100-110-, and 50-kDa polypeptides of the assembly protein, the clathrin β-light chain, and to a lesser extent the clathrin α-light chain. The phosphorylation of the assembled (particulate) and unassembled (soluble) pools of clathrin and assembly protein was compared by immunoprecipitating the respective protein complexes from particulate and soluble cell fractions. Although all the phosphorylated polypeptides were present in both fractions, the extent of labeling was protein and fraction specific: the apparent specific activities of the assembly protein 50-kDa polypeptide and clathrin light chain were higher in the unassembled pool, whereas those of the 100-110-kDa polypeptides were higher in the assembled pool. The amino acids and polypeptide fragments labeled in vivo appeared similar to those labeled in vitro.

Original languageEnglish
Pages (from-to)4408-4415
JournalJournal of Biological Chemistry
Volume263
Issue number9
StatePublished - 1 Jan 1988
Externally publishedYes

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