ATP binding by proteasomal ATPases regulates cellular assembly and substrate-induced functions of the 26 S proteasome

Young Chan Kim, Xiaohua Li, David Thompson, George N. Demartino

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

Background: ATPase subunits mediate 26 S proteasome assembly and function. Results: Defective ATP binding by some ATPase subunits inhibits proteasome assembly, and proteasomes harboring an ATP binding-defective subunit are impaired for proteolysis, substrate-stimulated gating, and ATPase activity. Conclusion: The proteasome requires normal ATP binding for assembly and function. Significance: Protein substrates promote their own degradation by inducing ATP-dependent proteasome functions.

Original languageEnglish (US)
Pages (from-to)3334-3345
Number of pages12
JournalJournal of Biological Chemistry
Volume288
Issue number5
DOIs
StatePublished - Feb 1 2013

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Proteasome Endopeptidase Complex
Adenosine Triphosphatases
Adenosine Triphosphate
Substrates
Proteolysis
Degradation
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

ATP binding by proteasomal ATPases regulates cellular assembly and substrate-induced functions of the 26 S proteasome. / Kim, Young Chan; Li, Xiaohua; Thompson, David; Demartino, George N.

In: Journal of Biological Chemistry, Vol. 288, No. 5, 01.02.2013, p. 3334-3345.

Research output: Contribution to journalArticle

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