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Dissociation of clathrin coats coupled to the hydrolysis of atp - role of an uncoating atpase

Academic Article
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Overview

authors

  • Braell, W. A.
  • Schlossman, D. M.
  • Schmid, Sandra
  • Rothman, J. E.

publication date

  • 1984

journal

  • Journal of Cell Biology  Journal

abstract

  • ATP hydrolysis was used to power the enzymatic release of clathrin from coated vesicles. The 70,000-mol-wt protein, purified on the basis of its ATP-dependent ability to disassemble clathrin cages, was found to possess a clathrin-dependent ATPase activity. Hydrolysis was specific for ATP; neither dATP nor other ribonucleotide triphosphates would either substitute for ATP or inhibit the hydrolysis of ATP in the presence of clathrin cages. The ATPase activity is elicited by clathrin in the form of assembled cages, but not by clathrin trimers, the product of cage disassembly. The 70,000-mol-wt polypeptide, but not clathrin, was labeled by ATP in photochemical cross-linking, indicating that the hydrolytic site for ATP resides on the uncoating protein. Conditions of low pH or high magnesium concentration uncouple ATP hydrolysis from clathrin release, as ATP is hydrolyzed although essentially no clathrin is released. This suggests that the recognition event triggering clathrin-dependent ATP hydrolysis occurs in the absence of clathrin release, and presumably precedes such release.

subject areas

  • Adenosine Triphosphatases
  • Adenosine Triphosphate
  • Animals
  • Binding Sites
  • Cations, Divalent
  • Cattle
  • Clathrin
  • Coated Pits, Cell-Membrane
  • Endosomes
  • Hydrogen-Ion Concentration
  • Kinetics
  • Osmolar Concentration
  • Protein Binding
  • Ribonucleotides
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Identity

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.99.2.734

PubMed ID

  • 6146631
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Additional Document Info

start page

  • 734

end page

  • 741

volume

  • 99

issue

  • 2

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