The ATPase core of a clathrin uncoating protein

T. G. Chappell, B. B. Konforti, S. L. Schmid, J. E. Rothman

Research output: Contribution to journalArticle

216 Scopus citations

Abstract

Chymotryptic digestion of bovine brain uncoating ATPase produced a 60-kDa fragment that was subsequently proteolyzed to 44 kDa. Loss of clathrin cage uncoating activity paralleled the conversion of the intact 70-kDa enzyme to the 60-kDa fragment, while clathrin binding activity was lost as the 60-kDa fragment was degraded to 44 kDa. This 44-kDa fragment has been purified to homogeneity and characterized as a clathrin-independent ATPase. The 44-kDa ATPase domain has been localized within the intact enzyme by the use of amino-terminal specific antibodies. This localization relates to the conserved nature of the 70-kDa heat shock protein family, of which bovine brain uncoating ATPase is a constitutively expressed member.

Original languageEnglish (US)
Pages (from-to)746-751
Number of pages6
JournalJournal of Biological Chemistry
Volume262
Issue number2
StatePublished - Jan 1 1987

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Chappell, T. G., Konforti, B. B., Schmid, S. L., & Rothman, J. E. (1987). The ATPase core of a clathrin uncoating protein. Journal of Biological Chemistry, 262(2), 746-751.