Selective externalization of an ATP-binding protein structurally related to the clathrin-uncoating ATPase/heat shock protein in vesicles containing terminal transferrin receptors during reticulocyte maturation.

Published

Journal Article

Transferrin receptors are lost from reticulocytes in vesicles that are released during the final stage of erythrocyte maturation (Pan, B. T., and Johnstone, R. M. (1983) Cell 33, 967-977). Transferrin receptor-containing vesicles have a major protein component present in a 1:1 ratio with the receptor that migrates on sodium dodecyl sulfate gels as two polypeptides of Mr = 71,000 and 72,000. The Mr = 71,000/72,000 doublet is indistinguishable from the clathrin-uncoating ATPase/heat shock protein based on cross-reaction with affinity-purified antibody against the uncoating protein, by comparison of peptide maps of the Mr = 72,000 and 71,000 polypeptides and the uncoating protein, and by selective binding of these polypeptides to ATP-agarose. This finding suggests a possible activity of proteins related to the uncoating/heat shock protein family in the disposal of aged membrane proteins by a pathway independent of lysosomes.

Full Text

Duke Authors

Cited Authors

  • Davis, JQ; Dansereau, D; Johnstone, RM; Bennett, V

Published Date

  • November 25, 1986

Published In

Volume / Issue

  • 261 / 33

Start / End Page

  • 15368 - 15371

PubMed ID

  • 3536900

Pubmed Central ID

  • 3536900

International Standard Serial Number (ISSN)

  • 0021-9258

Language

  • eng

Conference Location

  • United States