Landraud Luce, Pulcini Celine, Gounon Pierre, Flatau Gilles, Boquet Patrice, Lemichez Emmanuel
INSERM U452, Faculté de Médecine de Nice, Nice, France.
Int J Med Microbiol. 2004 Apr;293(7-8):513-8. doi: 10.1078/1438-4221-00295.
The cytotoxic necrotizing factor-1 (CNF1), a bacterial toxin of uropathogenic bacteria (UPEC), hijacks cellular Rho proteins of the Ras GTPase super-family. Recently, we have made three important findings. First, we have established that, following Rho protein activation by deamidation, these cellular proteins are ubiquitylated and degraded by the proteasome. Second, the low level of activated Rho proteins which results from the dual molecular mechanism of action of CNF1 (Rho protein activation followed by their degradation), confers high invasive properties to UPECs. Finally, we have reported that ubiquitylation and degradation of Rac is lost in HEp-2 carcinoma cells, thereby suggesting a possible link between Rho protein ubiquitylation and tumor progression.
细胞毒性坏死因子-1(CNF1)是一种尿路致病性大肠杆菌(UPEC)的细菌毒素,它劫持Ras GTPase超家族的细胞Rho蛋白。最近,我们有三项重要发现。第一,我们已经确定,在Rho蛋白通过脱酰胺作用激活后,这些细胞蛋白会被泛素化并被蛋白酶体降解。第二,CNF1的双重分子作用机制(Rho蛋白激活后随之降解)导致的低水平活化Rho蛋白赋予UPEC高侵袭性。最后,我们报告称,在HEp-2癌细胞中Rac的泛素化和降解缺失,从而表明Rho蛋白泛素化与肿瘤进展之间可能存在联系。