KEGG   PATHWAY: sfa03050
Entry
sfa03050                    Pathway                                
Name
Proteasome - Streptomyces pratensis
Description
The proteasome is a protein-destroying apparatus involved in many essential cellular functions, such as regulation of cell cycle, cell differentiation, signal transduction pathways, antigen processing for appropriate immune responses, stress signaling, inflammatory responses, and apoptosis. It is capable of degrading a variety of cellular proteins in a rapid and timely fashion and most substrate proteins are modified by ubiquitin before their degradation by the proteasome. The proteasome is a large protein complex consisting of a proteolytic core called the 20S particle and ancillary factors that regulate its activity in various ways. The most common form is the 26S proteasome containing one 20S core particle and two 19S regulatory particles that enable the proteasome to degrade ubiquitinated proteins by an ATP-dependent mechanism. Another form is the immunoproteasome containing two 11S regulatory particles, PA28 alpha and PA28 beta, which are induced by interferon gamma under the conditions of intensified immune response. Other regulatory particles include PA28 gamma and PA200. Although PA28 gamma also belongs to a family of activators of the 20S proteasome, it is localized within the nucleus and forms a homoheptamer. PA28 gamma has been implicated in the regulation of cell cycle progression and apoptosis. PA200 has been identified as a large nuclear protein that stimulates proteasomal hydrolysis of peptides.
Class
Genetic Information Processing; Folding, sorting and degradation
Pathway map
sfa03050  Proteasome
sfa03050

Other DBs
GO: 0000502
Organism
Streptomyces pratensis [GN:sfa]
Gene
Sfla_5188  AAA ATPase central domain protein [KO:K13527]
Sfla_5193  20S proteasome A and B subunits [KO:K03432] [EC:3.4.25.1]
Sfla_5192  20S proteasome A and B subunits [KO:K03433] [EC:3.4.25.1]
Reference
  Authors
Hirano Y, Murata S, Tanaka K
  Title
Large- and small-scale purification of mammalian 26S proteasomes.
  Journal
Methods Enzymol 399:227-40 (2005)
DOI:10.1016/S0076-6879(05)99015-0
Reference
  Authors
Saeki Y, Tanaka K
  Title
Cell biology: two hands for degradation.
  Journal
Nature 453:460-1 (2008)
DOI:10.1038/453460a
Reference
  Authors
Smith DM, Benaroudj N, Goldberg A
  Title
Proteasomes and their associated ATPases: a destructive combination.
  Journal
J Struct Biol 156:72-83 (2006)
DOI:10.1016/j.jsb.2006.04.012
Reference
  Authors
Strehl B, Seifert U, Kruger E, Heink S, Kuckelkorn U, Kloetzel PM
  Title
Interferon-gamma, the functional plasticity of the ubiquitin-proteasome system, and MHC class I antigen processing.
  Journal
Immunol Rev 207:19-30 (2005)
DOI:10.1111/j.0105-2896.2005.00308.x
Reference
  Authors
Darwin KH
  Title
Prokaryotic ubiquitin-like protein (Pup), proteasomes and pathogenesis.
  Journal
Nat Rev Microbiol 7:485-91 (2009)
DOI:10.1038/nrmicro2148
Reference
  Authors
Tomko RJ Jr, Hochstrasser M
  Title
Molecular architecture and assembly of the eukaryotic proteasome.
  Journal
Annu Rev Biochem 82:415-45 (2013)
DOI:10.1146/annurev-biochem-060410-150257
Reference
  Authors
Budenholzer L, Cheng CL, Li Y, Hochstrasser M
  Title
Proteasome Structure and Assembly.
  Journal
J Mol Biol 429:3500-3524 (2017)
DOI:10.1016/j.jmb.2017.05.027
Reference
  Authors
Cloos J, Roeten MS, Franke NE, van Meerloo J, Zweegman S, Kaspers GJ, Jansen G
  Title
(Immuno)proteasomes as therapeutic target in acute leukemia.
  Journal
Cancer Metastasis Rev 36:599-615 (2017)
DOI:10.1007/s10555-017-9699-4
Reference
  Authors
Sakata E, Bohn S, Mihalache O, Kiss P, Beck F, Nagy I, Nickell S, Tanaka K, Saeki Y, Forster F, Baumeister W
  Title
Localization of the proteasomal ubiquitin receptors Rpn10 and Rpn13 by electron cryomicroscopy.
  Journal
Proc Natl Acad Sci U S A 109:1479-84 (2012)
DOI:10.1073/pnas.1119394109
KO pathway
ko03050   

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