Hypothesis:: a glycoprotein-degradation complex formed by protein-protein interaction involves cytoplasmic peptide:N-glycanase
Hypothesis:: a glycoprotein-degradation complex formed by protein-protein interaction involves cytoplasmic peptide:N-glycanase
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DOI：
10.1016/s0006-291x(03)00052-4
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发表时间：
2003-02-28
影响因子：
3.1
通讯作者：
Lennarz, WJ
中科院分区：
文献类型：
--
作者：
Suzuki, T;Lennarz, WJ
一种细胞质多肽：N-葡聚糖酶与新合成的错误折叠糖蛋白的蛋白酶体降解有关，这些错误折叠的糖蛋白从内质网输出到胞浆中。最近，编码该酶的基因(Png1p)在酵母中被发现，并被证明通过与DNA修复系统的一个组成部分Rad23p相互作用而与26S蛋白酶体结合。此外，小鼠Png1p的同源物(MPng1p)具有扩展的N-末端结构域，被发现不仅与RAD23蛋白结合，而且还与泛素/蛋白酶体途径相关的各种蛋白结合。在酵母中没有发现的mPng1p的一个延伸的N末端含有一个潜在的蛋白质相互作用的部位，称为pub/pug结构域。PUB/PUG结构域被预测为富含螺旋，并存在于各种可能参与泛素/蛋白酶体相关途径的蛋白质中。本文将讨论N-葡聚糖酶在脱糖反应中的作用。在细胞过程中。此外，还将讨论PUB/PUG结构域对于形成假定的“糖蛋白-降解复合体”的潜在重要性。(C)2003年埃尔塞维尔科学公司(美国)。版权所有。
A cytoplasmic peptide:N-glycanase has been implicated in the proteasomal degradation of newly synthesized misfolded glycoproteins that are exported from the endoplasmic reticulum to the cytosol. Recently, the gene encoding this enzyme (Png1p) was identified in yeast and shown to bind to the 26S proteasome through its interaction with a component of the DNA repair system, Rad23p. Moreover, a mouse homologue of Png1p (mPng1p), which has an extended N-terminal domain, was found to bind not only to the Rad23 protein, but also to various proteins related to the ubiquitin/proteasome pathway. An extended N-terminus of mPng1p, which is not found in yeast, contains a potential site of protein-protein interaction called the PUB/PUG domain. The PUB/PUG domain is predicted to be helix-rich and is found in various proteins that may be involved in the ubiquitin/proteasome-related pathway. This review will discuss the consequence of the deglycosylation reaction by peptide:N-glycanase. in cellular processes. In addition, the potential importance of the PUB/PUG domain for the formation of a putative "glycoprotein-degradation complex" will be discussed. (C) 2003 Elsevier Science (USA). All rights reserved.