tailieunhanh - Báo cáo y học: " Proteomic view of mitochondrial function"

Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học Critical Care giúp cho các bạn có thêm kiến thức về ngành y học đề tài: Proteomic view of mitochondrial function. | Minireview Proteomic view of mitochondrial function Kai Stefan Dimmer and Doron Rapaport Address Interfakultares Institut fur Biochemie Hoppe-Seyler-Strasse University of Tubingen 72076 Tubingen Germany. Correspondence Doron Rapaport. Email Published 29 February 2008 Genome Biology 2008 9 209 doi gb-2008-9-2-209 The electronic version of this article is the complete one and can be found online at http 2008 9 2 209 2008 BioMed Central Ltd Abstract Genomic and proteomic studies have identified hundreds of proteins from mitochondria. A recent study has added a functional twist to these systematic approaches and identified novel mitochondrial modifiers and regulators. Mitochondria are ubiquitous and essential organelles in all eukaryotes and have many functions other than their main task of producing ATP. Besides the production of energy by cellular respiration mitochondria host the tricarboxylic acid cycle TCA cycle and the P-oxidation of fatty acids. In addition anabolic processes such as the biosynthesis of heme amino acids and lipids take place inside the organelle. Mitochondria are also pivotal for the production of iron-sulfur clusters for the entire eukaryotic cell 1 . Altogether these organelles are involved in a myriad of different processes as summarized in Figure 1. The shape of the mitochondrial network is sustained by three basic processes - fusion fission and active transport of the organelle along the cytoskeleton. To carry out these functions a mitochondrion is composed of hundreds of different proteins most of which are encoded by genes in the nucleus. To better understand the complexity of mitochondrial functions we need to identify all the mitochondrial components and to unravel the cytoplasmic signaling pathways that regulate the organelle s activities. To these ends various systematic approaches to mitochondrial protein identification have been undertaken in the past ten years. While most of