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本文引用的文献

1
Cluster formation of transmembrane proteins due to hydrophobic mismatching.由于疏水不匹配导致跨膜蛋白的聚簇形成。
Phys Rev Lett. 2008 Sep 19;101(12):128104. doi: 10.1103/PhysRevLett.101.128104.
2
Transmembrane domain-dependent partitioning of membrane proteins within the endoplasmic reticulum.内质网中膜蛋白的跨膜结构域依赖性分配
J Cell Biol. 2008 Apr 7;181(1):105-18. doi: 10.1083/jcb.200710093.
3
Palmitoylation and ubiquitination regulate exit of the Wnt signaling protein LRP6 from the endoplasmic reticulum.棕榈酰化和泛素化调节Wnt信号蛋白LRP6从内质网的输出。
Proc Natl Acad Sci U S A. 2008 Apr 8;105(14):5384-9. doi: 10.1073/pnas.0710389105. Epub 2008 Mar 31.
4
Palmitoylation: policing protein stability and traffic.棕榈酰化:调控蛋白质稳定性与运输
Nat Rev Mol Cell Biol. 2007 Jan;8(1):74-84. doi: 10.1038/nrm2084.
5
Size-dependent diffusion of membrane inclusions.膜内含物的尺寸依赖性扩散。
Biophys J. 2006 Oct 1;91(7):2393-8. doi: 10.1529/biophysj.106.087031. Epub 2006 Jul 7.
6
Sterols regulate ER-export dynamics of secretory cargo protein ts-O45-G.固醇调节分泌性货物蛋白ts-O45-G的内质网输出动态。
EMBO J. 2006 Jul 12;25(13):2953-65. doi: 10.1038/sj.emboj.7601205. Epub 2006 Jun 22.
7
Secretory cargo regulates the turnover of COPII subunits at single ER exit sites.分泌性货物在单个内质网出口位点调节COPII亚基的周转。
Curr Biol. 2006 Jan 24;16(2):173-9. doi: 10.1016/j.cub.2005.11.076.
8
Depalmitoylated Ras traffics to and from the Golgi complex via a nonvesicular pathway.去棕榈酰化的Ras通过非囊泡途径在高尔基体复合体之间运输。
J Cell Biol. 2005 Jul 18;170(2):261-72. doi: 10.1083/jcb.200502063.
9
Constant-pressure and constant-surface tension simulations in dissipative particle dynamics.耗散粒子动力学中的恒压和恒表面张力模拟。
J Chem Phys. 2005 Mar 22;122(12):124901. doi: 10.1063/1.1867374.
10
An acylation cycle regulates localization and activity of palmitoylated Ras isoforms.酰化循环调节棕榈酰化Ras亚型的定位和活性。
Science. 2005 Mar 18;307(5716):1746-52. doi: 10.1126/science.1105654. Epub 2005 Feb 10.

关于跨膜蛋白酰化作用的角色。

On the role of acylation of transmembrane proteins.

机构信息

German Cancer Research Center, Heidelberg, Germany.

出版信息

Biophys J. 2010 Mar 3;98(5):800-4. doi: 10.1016/j.bpj.2009.11.014.

DOI:10.1016/j.bpj.2009.11.014
PMID:20197033
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2830467/
Abstract

Acylation is a frequent means to ensure membrane association of a variety of soluble proteins in living cells. However, many transmembrane proteins are palmitoylated, indicating that this posttranslational modification may also serve as a means to regulate protein trafficking. Based on coarse-grained membrane simulations, we find that protein acylation significantly alters the tilting of transmembrane proteins with respect to the bilayer normal. In addition, the proteins' partitioning behavior and cluster formation ability due to hydrophobic mismatching is strongly altered. Based on our results, we propose that acylation is a potent means to regulate the trafficking of transmembrane proteins along the early secretory pathway.

摘要

酰化作用是确保活细胞中各种可溶性蛋白与膜结合的常用手段。然而,许多跨膜蛋白都发生了棕榈酰化,这表明这种翻译后修饰也可能作为调节蛋白运输的一种方式。基于粗粒化膜模拟,我们发现蛋白酰化会显著改变跨膜蛋白相对于双层膜法线的倾斜角度。此外,由于疏水性失配,蛋白质的分配行为和聚集体形成能力也会发生强烈改变。基于我们的结果,我们提出酰化作用是调节跨膜蛋白在早期分泌途径中运输的一种有效手段。