ATP-dependent mechanisms for protein degradation in mammalian cells.

G. N. DeMartino, M. J. McGuire, J. F. Reckelhoff, M. L. McCullough, D. E. Croall

Research output: Contribution to journalReview article

1 Scopus citations

Abstract

The biochemical basis for ATP-dependent protein degradation observed in intact cells has been studied in cell-free extracts of baby hamster kidney fibroblasts. ATP plays at least two distinct roles in proteolysis. First, ATP is required for the covalent conjugation of ubiquitin to protein substrates. This modification markedly enhances the rates of degradation of some, but not all, proteins. Second, ATP appears to stimulate the activity of a protease capable of degrading both ubiquitinated and non-ubiquitinated proteins. This protease has several biochemical and catalytic features that resemble those of the previously described high molecular weight protease, macropain. Furthermore, antibodies against highly purified human erythrocyte macropain inhibit both ubiquitin-dependent and ubiquitin-independent pathways of ATP-dependent proteolysis. Such results provide evidence for an important role for macropain in ATP-dependent proteolysis in mammalian cells.

Original languageEnglish (US)
Pages (from-to)181-196
Number of pages16
JournalRevisiones sobre biologia celular : RBC
Volume20
StatePublished - Dec 1 1989

ASJC Scopus subject areas

  • Medicine(all)

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    DeMartino, G. N., McGuire, M. J., Reckelhoff, J. F., McCullough, M. L., & Croall, D. E. (1989). ATP-dependent mechanisms for protein degradation in mammalian cells. Revisiones sobre biologia celular : RBC, 20, 181-196.