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细胞质 N-聚糖:泛素化导向蛋白酶体和自噬降解的触发物:监测细胞质 N-聚糖作为不需要的蛋白质和细胞器信号的分子系统。

Cytosolic N-Glycans: Triggers for Ubiquitination Directing Proteasomal and Autophagic Degradation: Molecular Systems for Monitoring Cytosolic N-Glycans as Signals for Unwanted Proteins and Organelles.

机构信息

Ubiquitin Project Tokyo Metropolitan Institute of Medical Science, 2-1-6, Kamikitazawa, Setagaya-ku, Tokyo, 156-8506, Japan.

Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, 2-1-6, Kamikitazawa, Setagaya-ku, Tokyo, 156-8506, Japan.

出版信息

Bioessays. 2018 Mar;40(3). doi: 10.1002/bies.201700215. Epub 2018 Feb 13.

Abstract

Proteins on the cell surface and secreted proteins are modified with sugar chains that generate and modulate biological complexity and diversity. Sugar chains not only contribute physically to the conformation and solubility of proteins, but also exert various functions via sugar-binding proteins (lectins) that reside on the cell surface or in organelles of the secretory pathway. However, some glycosidases and lectins are found in the cytosol or nucleus. Recent studies of cytosolic sugar-related molecules have revealed that sugar chains on proteins in the cytosol act as signals of adverse cellular conditions. In this review, we summarize recent reports that cytosolic sugar chains can trigger ubiquitination, followed by proteasomal and autophagic degradation to maintain cellular homeostasis. In addition, we discuss the functions of sugar-binding proteins revealed to date, along with possibilities not yet explored.

摘要

细胞表面蛋白和分泌蛋白通过糖链修饰,从而产生和调节生物复杂性和多样性。糖链不仅对蛋白质的构象和溶解度有物理贡献,而且还通过位于细胞表面或分泌途径细胞器中的糖结合蛋白(凝集素)发挥各种功能。然而,一些糖苷酶和凝集素存在于细胞质或核内。最近对细胞质中与糖相关的分子的研究表明,细胞质中蛋白质上的糖链可以作为细胞不良状态的信号。在这篇综述中,我们总结了最近的报告,即细胞质中的糖链可以触发泛素化,随后进行蛋白酶体和自噬降解,以维持细胞内稳态。此外,我们还讨论了迄今为止发现的糖结合蛋白的功能,以及尚未探索的可能性。

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