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The murine cardiac 26S proteasome: an organelle awaiting exploration.

Authors :
Gomes AV
Zong C
Edmondson RD
Berhane BT
Wang GW
Le S
Young G
Zhang J
Vondriska TM
Whitelegge JP
Jones RC
Joshua IG
Thyparambil S
Pantaleon D
Qiao J
Loo J
Ping P
Source :
Annals of the New York Academy of Sciences [Ann N Y Acad Sci] 2005 Jun; Vol. 1047, pp. 197-207.
Publication Year :
2005

Abstract

Multiprotein complexes have been increasingly recognized as essential functional units for a variety of cellular processes, including the protein degradation system. Selective degradation of proteins in eukaryotes is primarily conducted by the ubiquitin proteasome system. The current knowledge base, pertaining to the proteasome complexes in mammalian cells, relies largely upon information gained in the yeast system, where the 26S proteasome is hypothesized to contain a 20S multiprotein core complex and one or two 19S regulatory complexes. To date, the molecular structure of the proteasome system, the proteomic composition of the entire 26S multiprotein complexes, and the specific designated function of individual components within this essential protein degradation system in the heart remain virtually unknown. A functional proteomic approach, employing multidimensional chromatography purification combined with liquid chromatography tandem mass spectrometry and protein chemistry, was utilized to explore the murine cardiac 26S proteasome system. This article presents an overview on the subject of protein degradation in mammalian cells. In addition, this review shares the limited information that has been garnered thus far pertaining to the molecular composition, function, and regulation of this important organelle in the cardiac cells.

Details

Language :
English
ISSN :
0077-8923
Volume :
1047
Database :
MEDLINE
Journal :
Annals of the New York Academy of Sciences
Publication Type :
Academic Journal
Accession number :
16093497
Full Text :
https://doi.org/10.1196/annals.1341.018