title: The murine cardiac 26S proteasome: an organelle awaiting exploration.
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.
authors.affiliation: Department of Physiology and Medicine, and Cardiac Proteomics and Signaling Lab at the Cardiovascular Research Laboratory, University of California at Los Angeles, School of Medicine, Los Angeles, California 90095, USA.
authors.forename: Aldrin V
authors.initials: AV
authors.lastname: Gomes
authors.forename: Chenggong
authors.initials: C
authors.lastname: Zong
authors.forename: Ricky D
authors.initials: RD
authors.lastname: Edmondson
authors.forename: Beniam T
authors.initials: BT
authors.lastname: Berhane
authors.forename: Guang-Wu
authors.initials: GW
authors.lastname: Wang
authors.forename: Steven
authors.initials: S
authors.lastname: Le
authors.forename: Glen
authors.initials: G
authors.lastname: Young
authors.forename: Jun
authors.initials: J
authors.lastname: Zhang
authors.forename: Thomas M
authors.initials: TM
authors.lastname: Vondriska
authors.forename: Julian P
authors.initials: JP
authors.lastname: Whitelegge
authors.forename: Richard C
authors.initials: RC
authors.lastname: Jones
authors.forename: Irving G
authors.initials: IG
authors.lastname: Joshua
authors.forename: Sheeno
authors.initials: S
authors.lastname: Thyparambil
authors.forename: Dawn
authors.initials: D
authors.lastname: Pantaleon
authors.forename: Joe
authors.initials: J
authors.lastname: Qiao
authors.forename: Joseph
authors.initials: J
authors.lastname: Loo
authors.forename: Peipei
authors.initials: P
authors.lastname: Ping
mesh_terms: D000818:Animals; D051379:Mice; D009206:Myocardium / Q000737:chemistry / Q000378:metabolism*; D015388:Organelles / Q000737:chemistry / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex / Q000737:chemistry / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism; D025801:Ubiquitin / Q000378:metabolism
chemical_list: D011506:Proteins; D025801:Ubiquitin; D046988:Proteasome Endopeptidase Complex; C061553:ATP dependent 26S protease