Regulation of proteasome complexes by gamma-interferon and phosphorylation (Q28211514)

Structure and functions of the 20S and 26S proteasomes

Europe PubMed Central

title

Regulation of proteasome complexes by gamma-interferon and phosphorylation (English)

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A J Rivett

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S Bose

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2

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P Brooks

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3

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K I Broadfoot

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4

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language of work or name

English

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publication date

2001

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83

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issue

3-4

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page(s)

363-6

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cites work

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Structure of 20S proteasome from yeast at 2.4 A resolution

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The proteasome, a novel protease regulated by multiple mechanisms

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The proteasome activator 11 S REG (PA28) and class I antigen presentation

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Degradation of cell proteins and the generation of MHC class I-presented peptides

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Impaired immunoproteasome assembly and immune responses in PA28-/- mice.

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Subcellular localization of proteasomes and their regulatory complexes in mammalian cells.

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Electron microscopic localization of the multicatalytic proteinase complex in rat liver and in cultured cells

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Subpopulations of proteasomes in rat liver nuclei, microsomes and cytosol

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Localization of the 26S proteasome during mitosis and meiosis in fission yeast

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Association of immunoproteasomes with the endoplasmic reticulum

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Dynamics of proteasome distribution in living cells

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Location of MHC-encoded transporters in the endoplasmic reticulum and cis-Golgi.

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gamma-Interferon decreases the level of 26 S proteasomes and changes the pattern of phosphorylation

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Simultaneous binding of PA28 and PA700 activators to 20 S proteasomes

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Hybrid proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis

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Phosphorylation of C8 and C9 subunits of the multicatalytic proteinase by casein kinase II and identification of the C8 phosphorylation sites by direct mutagenesis

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Phosphorylation of proteasomes in mammalian cells. Identification of two phosphorylated subunits and the effect of phosphorylation on activity

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Phosphorylation of ATPase subunits of the 26S proteasome

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Phosphorylation of proteasomes in mammalian cells

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In vivo assembly of the proteasomal complexes, implications for antigen processing

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