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细胞通过修饰氨基末端控制蛋白质周转。

Cellular Control of Protein Turnover via the Modification of the Amino Terminus.

机构信息

Max Perutz Labs, Department of Biochemistry and Cell Biology, University of Vienna, A-1030 Vienna, Austria.

Vienna BioCenter, Research Institute of Molecular Pathology, A-1030 Vienna, Austria.

出版信息

Int J Mol Sci. 2021 Mar 29;22(7):3545. doi: 10.3390/ijms22073545.

DOI:10.3390/ijms22073545
PMID:33805528
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8037982/
Abstract

The first amino acid of a protein has an important influence on its metabolic stability. A number of ubiquitin ligases contain binding domains for different amino-terminal residues of their substrates, also known as N-degrons, thereby mediating turnover. This review summarizes, in an exemplary way, both older and more recent findings that unveil how destabilizing amino termini are generated. In most cases, a step of proteolytic cleavage is involved. Among the over 500 proteases encoded in the genome of higher eukaryotes, only a few are known to contribute to the generation of N-degrons. It can, therefore, be expected that many processing paths remain to be discovered.

摘要

蛋白质的第一个氨基酸对其代谢稳定性有重要影响。许多泛素连接酶包含与其底物不同氨基末端残基的结合结构域,也称为 N 降解元件,从而介导周转率。本综述以示例的方式总结了揭示不稳定氨基末端如何产生的较旧和更新的发现。在大多数情况下,涉及蛋白水解切割的步骤。在高等真核生物基因组中编码的超过 500 种蛋白酶中,只有少数已知有助于 N 降解元件的生成。因此,可以预期许多加工途径仍有待发现。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/37a5/8037982/caffd7fcdeff/ijms-22-03545-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/37a5/8037982/caffd7fcdeff/ijms-22-03545-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/37a5/8037982/caffd7fcdeff/ijms-22-03545-g001.jpg

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