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首页> 外文期刊>Journal of Cell Science >N epsilon-lysine acetylation in the endoplasmic reticulum - a novel cellular mechanism that regulates proteostasis and autophagy
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N epsilon-lysine acetylation in the endoplasmic reticulum - a novel cellular mechanism that regulates proteostasis and autophagy

机译：Nε-赖氨酸乙酰化在内质网中 - 一种调节蛋白质和自噬的新细胞机制

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摘要

Protein post-translational modifications (PTMs) take many shapes, have many effects and are necessary for cellular homeostasis. One of these PTMs, N epsilon-lysine acetylation, was thought to occur only in the mitochondria, cytosol and nucleus, but this paradigm was challenged in the past decade with the discovery of lysine acetylation in the lumen of the endoplasmic reticulum (ER). This process is governed by the ER acetylation machinery: the cytosol: ER-lumen acetyl-CoA transporter AT-1 (also known as SLC33A1), and the ER-resident lysine acetyltransferases ATase1 and ATase2 (also known as NAT8B and NAT8, respectively). This Review summarizes the more recent biochemical, cellular and mouse model studies that underscore the importance of the ER acetylation process in maintaining protein homeostasis and autophagy within the secretory pathway, and its impact on developmental and age-associated diseases.
机译：蛋白质翻译后修饰（PTMS）采取多种形状，具有许多效果，并且是细胞稳态所必需的。 认为这些PTMS Nε-赖氨酸乙酰化仅在线粒体，细胞溶溶胶和核中发生，但在过去十年中，这种范例在半质网（ER）内腔中的赖氨酸乙酰化发现赖氨酸乙酰化攻击。 该过程由ER乙酰化机械控制：胞嘧啶：ER-j乙酰-CoA转运蛋白，AT-1（也称为SLC33A1），以及ATase1和Atase2的ER-驻留赖氨酸乙酰转移酶（分别称为NAT8B和NAT8） 。 本综述总结了最近的生物化学，细胞和小鼠模型研究，以强调ER乙酰化过程在分泌途径内维持蛋白质稳态和自噬的重要性，以及其对发育和年龄相关疾病的影响。

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