In vivo characterization of the proteasome regulator PA28

Kwangseog Ahn, Mark Erlander, Didier Leturcq, Per A. Peterson, Klaus Früh, Young Yang

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Abstract

A proteasome regulator, termed PA28, has been shown to modulate peptidase activities of the proteasomes in vitro. Two different but homologous PA28 molecules, designated as PA28α and PA28β, have been cloned. Both a and β polypeptides of PA28 are found in PA28 complexes isolated from cells, indicating that both are constituents of functional PA28 complexes. Using antisera specific to pA28α, PA28β, and epitope-tagged PA28 molecules, we show that expression of PA28α and PA28β is coordinately induced by various cytokines in different cell lines and that PA28 subunits and proteasomes have almost identical half-lives. In addition, we show that PA28 complexes are associated with 20 S but not 26 S proteasomes in vivo. Moreover, we demonstrate that PA28 complex is a heterohexamer composed of both α and β subunits with a stoichiometry of α3β3 in an alternating order.

Original languageEnglish (US)
Pages (from-to)18237-18242
Number of pages6
JournalJournal of Biological Chemistry
Volume271
Issue number30
DOIs
StatePublished - Aug 10 1996

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Ahn, K., Erlander, M., Leturcq, D., Peterson, P. A., Früh, K., & Yang, Y. (1996). In vivo characterization of the proteasome regulator PA28. Journal of Biological Chemistry, 271(30), 18237-18242. https://doi.org/10.1074/jbc.271.30.18237