Germain Doris
Mount Sinai School of Medicine, Division of Hematology/Oncology Box 1079, One Gustave L. Levy Place, New York, NY 11029, USA.
Mol Microbiol. 2008 Dec;70(6):1334-41. doi: 10.1111/j.1365-2958.2008.06502.x. Epub 2008 Oct 17.
The ubiquitin-independent protein quality control of matrix proteins of the mitochondrion is well characterized and until recently the mitochondrion was considered a 'ubiquitination-free' organelle. However, a number of studies now indicate multiple roles of the ubiquitin-proteasome pathway in the regulation and maintenance of mitochondrial integrity. Of particular interest to this review is the finding of a mitochondrial ubiquitin-dependent protein quality control and that this pathway may share similarity to the endoplasmic reticulum-associated degradation (ERAD) pathway that acts to eliminate misfolded proteins from the lumen of the endoplasmic reticulum. The potential cross-talk between the ubiquitin-dependent and -independent protein quality controls and their implications in ageing and neurodegenerative diseases, notably in Parkinson's disease, are discussed.
线粒体基质蛋白的泛素非依赖性蛋白质质量控制已得到充分表征，直到最近，线粒体还被认为是一个“无泛素化”的细胞器。然而，现在一些研究表明泛素 - 蛋白酶体途径在调节和维持线粒体完整性方面具有多种作用。本综述特别感兴趣的是发现了线粒体泛素依赖性蛋白质质量控制，并且该途径可能与内质网相关降解（ERAD）途径有相似之处，ERAD途径的作用是从内质网腔中清除错误折叠的蛋白质。本文讨论了泛素依赖性和非依赖性蛋白质质量控制之间的潜在相互作用及其在衰老和神经退行性疾病（尤其是帕金森病）中的意义。
