Instituto de Investigação e Inovação em Saúde (i3S), Instituto de Biologia Molecular e Celular (IBMC), Instituto de Ciências Biomédicas de Abel Salazar (ICBAS)-Universidade do Porto, Rua Alfredo Allen, 208, 4200-135 Porto, Portugal.
Int J Mol Sci. 2019 Oct 23;20(21):5246. doi: 10.3390/ijms20215246.
In contrast to many protein translocases that use ATP or GTP hydrolysis as the driving force to transport proteins across biological membranes, the peroxisomal matrix protein import machinery relies on a regulated self-assembly mechanism for this purpose and uses ATP hydrolysis only to reset its components. The ATP-dependent protein complex in charge of resetting this machinery-the Receptor Export Module (REM)-comprises two members of the "ATPases Associated with diverse cellular Activities" (AAA+) family, PEX1 and PEX6, and a membrane protein that anchors the ATPases to the organelle membrane. In recent years, a large amount of data on the structure/function of the REM complex has become available. Here, we discuss the main findings and their mechanistic implications.
与许多利用 ATP 或 GTP 水解作为驱动力将蛋白质穿过生物膜的蛋白质转运体不同,过氧化物酶体基质蛋白导入机制依赖于受调控的自组装机制来实现这一目的,并且仅利用 ATP 水解来重置其组件。负责重置该机制的 ATP 依赖性蛋白复合物——受体输出模块(REM)——包含两个“与多种细胞活动相关的 ATP 酶”(AAA+)家族成员 PEX1 和 PEX6,以及一个将 ATP 酶锚定到细胞器膜上的膜蛋白。近年来,有关 REM 复合物的结构/功能的大量数据已经可用。在这里,我们讨论了主要发现及其机制意义。