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Regulation of the endothelial cell cycle by the ubiquitin-proteasome system Fasanaro P; Capogrossi MC; Martelli FCardiovasc Res 2010[Jan]; 85 (2): 272-80Degradation of poly-ubiquitinated proteins by the 26S-proteasome complex represents a crucial quantitative control mechanism. The ubiquitin-proteasome system (UPS) plays a pivotal role in the complex molecular network regulating the progression both between and within each cell-cycle phase. Two major complexes are involved: the SKP1-CUL1-F-box-protein complex (SCF) and the anaphase-promoting complex/cyclosome (APC/C). Notwithstanding structural similarities, SCF and APC/C display different cellular functions and mechanisms of action. SCF modulates all cell-cycle stages and plays a prominent role at G1/S transition mainly through three regulatory subunits: Skp2, Fbw7, and beta-TRCP. APC/C, regulated by Cdc20 or Cdh1 subunits, has a crucial role in mitosis. In this review, we will describe how the endothelial cell cycle is regulated by the UPS. We will illustrate the principal SCF- and APC/C-dependent molecular mechanisms that modulate cell growth, allowing a unidirectional cell-cycle progression. Then, we will focus our attention on UPS modulation by oxidative stress, a pathogenic stimulus that causes endothelial dysfunction and is involved in numerous cardiovascular diseases.|*Cell Cycle[MESH]|Anaphase-Promoting Complex-Cyclosome[MESH]|Animals[MESH]|Cardiovascular Diseases/etiology[MESH]|Endothelial Cells/*cytology[MESH]|Humans[MESH]|NF-E2-Related Factor 2/physiology[MESH]|Oxidative Stress[MESH]|Proteasome Endopeptidase Complex/*physiology[MESH]|SKP Cullin F-Box Protein Ligases/*physiology[MESH]|Tumor Suppressor Protein p53/physiology[MESH]|Ubiquitin-Protein Ligase Complexes/*physiology[MESH]|Ubiquitin/*metabolism[MESH] |
