TY - JOUR
T1 - The murine cardiac 26S proteasome
T2 - An organelle awaiting exploration
AU - Gomes, Aldrin V
AU - Zong, Chenggong
AU - Edmondson, Ricky D.
AU - Berhane, Beniam T.
AU - Wang, Guang Wu
AU - Le, Steven
AU - Young, Glen
AU - Zhang, Jun
AU - Vondriska, Thomas M.
AU - Whitelegge, Julian P.
AU - Jones, Richard C.
AU - Joshua, Irving G.
AU - Thyparambil, Sheeno
AU - Pantaleon, Dawn
AU - Qiao, Joe
AU - Loo, Joseph
AU - Ping, Peipei
PY - 2005
Y1 - 2005
N2 - 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.
AB - 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.
KW - 26S proteasome
KW - Protein degradation
KW - Proteomics
KW - Ubiquitination
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U2 - 10.1196/annals.1341.018
DO - 10.1196/annals.1341.018
M3 - Article
C2 - 16093497
AN - SCOPUS:23744478678
VL - 1047
SP - 197
EP - 207
JO - Annals of the New York Academy of Sciences
JF - Annals of the New York Academy of Sciences
SN - 0077-8923
ER -