比较互作组分析揭示了 Raf 家族激酶的独特和重叠特性。

Comparative interactome analysis reveals distinct and overlapping properties of Raf family kinases.

机构信息

Faculty of Life Science and Technology, Kunming University of Science and Technology, Kunming, 650500, China.

Faculty of Life Science and Technology, Kunming University of Science and Technology, Kunming, 650500, China; Center of Stomatology, The First People's Hospital of Yunnan Province, Kunming, 650032, China; The Affiliated Hospital of Kunming University of Science and Technology, Kunming, 650032, China.

出版信息

Biochem Biophys Res Commun. 2019 Jul 5;514(4):1217-1223. doi: 10.1016/j.bbrc.2019.05.089. Epub 2019 May 18.

DOI:10.1016/j.bbrc.2019.05.089

PMID:31109650

Abstract

The three mammalian Raf proteins (A-Raf, B-Raf, and C-Raf) are key components of the MAPK pathway. Although diverse functions have been proposed for Raf kinases, it is still not clear how interacting proteins contribute to differences in the signaling functions of the three Raf kinases. Here, we report the comparative interactomes of the three Raf kinases under serum-starved and EGF-stimulated conditions. We identified nearly 400 novel interacting proteins; some interacted with all three isoforms while others interacted exclusively with one or two. Comparing the interactomes of the three Raf kinases under different conditions revealed Raf proteins perform distinct functions through specific interactions. Our interactome data help define the differences between the three Raf kinases and may uncover new functions or regulatory mechanisms. Knowledge of Raf kinase protein-protein interactions will help us to investigate the function of specific pathways in the future.

摘要

三种哺乳动物 Raf 蛋白（A-Raf、B-Raf 和 C-Raf）是 MAPK 途径的关键组成部分。尽管 Raf 激酶具有多种功能，但目前尚不清楚相互作用的蛋白质如何促成三种 Raf 激酶信号转导功能的差异。在这里，我们报告了在血清饥饿和 EGF 刺激条件下三种 Raf 激酶的比较相互作用组。我们鉴定了近 400 种新的相互作用蛋白；有些与所有三种同工型相互作用，而有些则仅与一种或两种相互作用。比较三种 Raf 激酶在不同条件下的相互作用组发现，Raf 蛋白通过特定的相互作用发挥不同的功能。我们的相互作用组数据有助于定义三种 Raf 激酶之间的差异，并可能揭示新的功能或调节机制。了解 Raf 激酶蛋白-蛋白相互作用将有助于我们在未来研究特定途径的功能。