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E3 泛素连接酶在 B 细胞恶性肿瘤中的作用。

E3 ubiquitin ligases in B-cell malignancies.

机构信息

Department of Cancer Biology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.

Department of Cancer Biology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.

出版信息

Cell Immunol. 2019 Jun;340:103905. doi: 10.1016/j.cellimm.2019.02.004. Epub 2019 Feb 26.

DOI:10.1016/j.cellimm.2019.02.004
PMID:30827673
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6584052/
Abstract

Ubiquitylation is a post-translational modification (PTM) that controls various cellular signaling pathways. It is orchestrated by a three-step enzymatic cascade know as the ubiquitin proteasome system (UPS). E3 ligases dictate the specificity to the substrates, primarily leading to proteasome-dependent degradation. Deregulation of the UPS components by various mechanisms contributes to the pathogenesis of cancer. This review focuses on E3 ligase-substrates pairings that are implicated in B-cell malignancies. Understanding the molecular mechanism of specific E3 ubiquitin ligases will present potential opportunities for the development of targeted therapeutic approaches.

摘要

泛素化是一种翻译后修饰(PTM),可控制各种细胞信号通路。它由一个三步酶级联反应调控,即泛素蛋白酶体系统(UPS)。E3 连接酶决定了底物的特异性,主要导致蛋白酶体依赖性降解。UPS 成分的各种机制失调导致癌症的发病机制。本综述重点介绍了参与 B 细胞恶性肿瘤的 E3 连接酶-底物配对。了解特定 E3 泛素连接酶的分子机制将为开发靶向治疗方法提供潜在机会。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9df7/6584052/b5346f495d9a/nihms-1522843-f0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9df7/6584052/1df157571bb2/nihms-1522843-f0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9df7/6584052/b5346f495d9a/nihms-1522843-f0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9df7/6584052/1df157571bb2/nihms-1522843-f0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9df7/6584052/b5346f495d9a/nihms-1522843-f0002.jpg

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