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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.

Publication ,  Journal Article
Davis, JQ; Dansereau, D; Johnstone, RM; Bennett, V
Published in: J Biol Chem
November 25, 1986

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.

Duke Scholars

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

November 25, 1986

Volume

261

Issue

33

Start / End Page

15368 / 15371

Location

United States

Related Subject Headings

  • Sheep
  • Reticulocytes
  • Receptors, Transferrin
  • Molecular Weight
  • Immunosorbent Techniques
  • Humans
  • Heat-Shock Proteins
  • HSP70 Heat-Shock Proteins
  • HSC70 Heat-Shock Proteins
  • Erythrocyte Membrane
 

Citation

APA
Chicago
ICMJE
MLA
NLM

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

November 25, 1986

Volume

261

Issue

33

Start / End Page

15368 / 15371

Location

United States

Related Subject Headings

  • Sheep
  • Reticulocytes
  • Receptors, Transferrin
  • Molecular Weight
  • Immunosorbent Techniques
  • Humans
  • Heat-Shock Proteins
  • HSP70 Heat-Shock Proteins
  • HSC70 Heat-Shock Proteins
  • Erythrocyte Membrane