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| Publications [#112964] of G Vann V. Bennett
Papers Published
- JQ Davis, D Dansereau, RM Johnstone, V Bennett, 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.,
The Journal of biological chemistry, UNITED STATES, vol. 261 no. 33
(November, 1986),
pp. 15368-71, ISSN 0021-9258
(last updated on 2003/02/18)
Abstract: 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.
Keywords: Animals • Carrier Proteins • Electrophoresis, Polyacrylamide Gel • Erythrocyte Membrane • HSC70 Heat-Shock Proteins • HSP70 Heat-Shock Proteins* • Heat-Shock Proteins • Humans • Immunosorbent Techniques • Molecular Weight • Receptors, Transferrin • Reticulocytes • Sheep • blood* • metabolism*
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