Lee Kang-Eun, Heo Ji-Eun, Kim Jeong-Mok, Hwang Cheol-Sang
Department of Life Sciences, Pohang University of Science and Technology, Pohang, Gyeongbuk 790-784, Korea.
Mol Cells. 2016 Mar;39(3):169-78. doi: 10.14348/molcells.2016.2329. Epub 2016 Feb 16.
Although Nα-terminal acetylation (Nt-acetylation) is a pervasive protein modification in eukaryotes, its general functions in a majority of proteins are poorly understood. In 2010, it was discovered that Nt-acetylation creates a specific protein degradation signal that is targeted by a new class of the N-end rule proteolytic system, called the Ac/N-end rule pathway. Here, we review recent advances in our understanding of the mechanism and biological functions of the Ac/N-end rule pathway, and its crosstalk with the Arg/N-end rule pathway (the classical N-end rule pathway).
尽管Nα-末端乙酰化(Nt-乙酰化)是真核生物中一种普遍存在的蛋白质修饰,但大多数蛋白质中其一般功能仍知之甚少。2010年,人们发现Nt-乙酰化会产生一种特定的蛋白质降解信号,该信号可被一类新的N-末端规则蛋白水解系统靶向识别,即Ac/N-末端规则途径。在此,我们综述了对Ac/N-末端规则途径的机制、生物学功能及其与Arg/N-末端规则途径(经典N-末端规则途径)相互作用的最新研究进展。