Matějíková J, Kubiczková L, Sedlaříková L, Potáčová A, Hájek R, Sevčíková S
Babákova myelomová skupina, Ústav patologické fyziologie, LF MU, Brno.
Klin Onkol. 2013;26(4):251-6. doi: 10.14735/amko2013251.
All intracellular and some extracellular proteins are continually degraded and replaced by synthesis of new proteins. Both these processes need to stay in equilibrium since their balance may lead to emergence of diseases. Cells contain many proteolytic systems that ensure highly specific and controlled degradation of proteins. One of these systems is the proteasome, a very complex molecular engine allowing degradation of proteins conjugated to ubiquitin. Since the first isolation of proteasome in 1968, many details about its function have been uncovered. In 2004, Nobel Prize for chemistry was awarded for these discoveries. In our review article, we aimed to summarize information about the mechanism of highly selective degradation of proteins by the ubiquitin proteasome pathway. Individual parts of the paper summarize current knowledge about highly selective degradation of proteins by the ubiquitin proteasome system, mechanisms of protein degradation regulation and bio-logical effects of proteasome inhibitors.
所有细胞内蛋白质以及一些细胞外蛋白质都在不断地被降解,并通过合成新蛋白质来替换。这两个过程需要保持平衡,因为它们的失衡可能会导致疾病的出现。细胞含有许多蛋白水解系统,以确保蛋白质进行高度特异性且受调控的降解。其中一个系统就是蛋白酶体,它是一个非常复杂的分子机器,能够使与泛素结合的蛋白质发生降解。自1968年首次分离出蛋白酶体以来,其功能的许多细节已被揭示。2004年,这些发现获得了诺贝尔化学奖。在我们的综述文章中,我们旨在总结关于泛素蛋白酶体途径对蛋白质进行高度选择性降解机制的信息。本文的各个部分总结了目前关于泛素蛋白酶体系统对蛋白质进行高度选择性降解的知识、蛋白质降解调控机制以及蛋白酶体抑制剂的生物学效应。