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蛋白质类异戊二烯化:一种新的宿主-病原体相互作用模式。

Protein prenylation: a new mode of host-pathogen interaction.

机构信息

School of Systems Biology, George Mason University, 10900 University Blvd, Manassas, VA 20110, USA.

出版信息

Biochem Biophys Res Commun. 2011 Dec 9;416(1-2):1-6. doi: 10.1016/j.bbrc.2011.10.142. Epub 2011 Nov 6.

Abstract

Post translational modifications are required for proteins to be fully functional. The three step process, prenylation, leads to farnesylation or geranylgeranylation, which increase the hydrophobicity of the prenylated protein for efficient anchoring into plasma membranes and/or organellar membranes. Prenylated proteins function in a number of signaling and regulatory pathways that are responsible for basic cell operations. Well characterized prenylated proteins include Ras, Rac and Rho. Recently, pathogenic prokaryotic proteins, such as SifA and AnkB, have been shown to be prenylated by eukaryotic host cell machinery, but their functions remain elusive. The identification of other bacterial proteins undergoing this type of host-directed post-translational modification shows promise in elucidating host-pathogen interactions to develop new therapeutics. This review incorporates new advances in the study of protein prenylation into a broader aspect of biology with a focus on host-pathogen interaction.

摘要

蛋白质的完全功能需要经过翻译后的修饰。三步过程—— prenylation( prenylation),导致 farnesylation 或 geranylgeranylation,增加 prenylated 蛋白的疏水性,使其有效地锚定到质膜和/或细胞器膜中。 prenylated 蛋白在许多信号和调节途径中发挥作用,这些途径负责细胞的基本运作。 well characterized prenylated 蛋白包括 Ras、Rac 和 Rho。最近,致病性原核蛋白,如 SifA 和 AnkB,已被证明被真核宿主细胞机制 prenylation,但它们的功能仍然难以捉摸。鉴定其他经历这种宿主定向翻译后修饰的细菌蛋白,有望阐明宿主-病原体相互作用,以开发新的治疗方法。本综述将蛋白质 prenylation 的新进展纳入生物学的更广泛方面,重点关注宿主-病原体相互作用。

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