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PMID: 11495792 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Review

PCI complexes: pretty complex interactions in diverse signaling pathways.

Trends in plant science ·Vol. 6 ·No. 8 ·2001-08-00 ·Pages 379-86

Kim T, Hofmann K, von Arnim AG, Chamovitz DA

Abstract

Three protein complexes (the proteasome regulatory lid, the COP9 signalosome and eukaryotic translation initiation factor 3) contain protein subunits with a well defined protein domain, the PCI domain. At least two (the COP9 signalosome and the lid) appear to share a common evolutionary origin. Recent advances in our understanding of the structure and function of the three complexes point to intriguing and unanticipated connections between the cellular functions performed by these three protein assemblies, especially between translation initiation and proteolytic protein degradation.

MeSH Terms
Animals COP9 Signalosome Complex Cysteine Endopeptidases/classification,genetics Eukaryotic Initiation Factor-3 Evolution, Molecular Multienzyme Complexes/classification,genetics Multiprotein Complexes Peptide Hydrolases Peptide Initiation Factors/classification,genetics Phylogeny Proteasome Endopeptidase Complex Protein Biosynthesis Proteins/classification,genetics Signal Transduction
Chemicals
Eukaryotic Initiation Factor-3 Multienzyme Complexes Multiprotein Complexes Peptide Initiation Factors Proteins Peptide Hydrolases COP9 Signalosome Complex Cysteine Endopeptidases Proteasome Endopeptidase Complex
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Kim T
Dept Botany, The University of Tennessee, Knoxville TN 37996-1100, USA.
Hofmann K
von Arnim A G
Chamovitz D A
Article Info
Journal
Trends in plant science
Abbr.
Trends Plant Sci
ISSN
1360-1385
Published
2001-08-00
Pages
379-86
Language
English
Region
England
NLM ID
9890299
Subset
IM
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