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血小板细丝蛋白:一种参与细胞信号整合与功能的细胞骨架蛋白

[Platelet filamin: a cytoskeletal protein involved in cell signal integration and function].

作者信息

García Elizabeth, Jay David

机构信息

Departamento de Biomedicina Cardiovascular, Instituto Nacional de Cardiología, Ignacio Chávez, México, D.F.

出版信息

Arch Cardiol Mex. 2006 Oct-Dec;76 Suppl 4:S67-75.

PMID:17469336
Abstract

Activation of cellular receptors by diverse stimuli induces dramatic changes in shape and function to respond to the new circumstances of the cell. This modified behavior depends on the reorganization of the peripheral actin meshwork. An outstanding example of these processes can be found in platelets, from which much of the information available on cytoskeletal function has been obtained. Among the many actin-crosslinking proteins like spectrin, fimbrin or alpha actinin, filamin a (FLNa) emerges as the one with the highest potential in initiating the polimerization of actin filaments (F-actin) during the formation of tridimensional actin gels. FLNa also links actin filaments to the cytosolic domain of many membrane glycoproteins in platelets through its C-terminal region. In addition to participating in cell shape changes, FLNa is a scaffoldding protein that recruits numerous proteins involved in a completely different set of functions, including signal transduction, gene transcription regulation, and receptor translocation; however, the physiological role of FLNa in these processes has remained elusive. The purpose of the present communication is to briefly describe the characteristics of the macromolecules able to interact with FLNa and to discuss a possible role of FLNa during the transduction of signals from those molecular elements in platelets.

摘要

多种刺激激活细胞受体可诱导细胞形态和功能发生显著变化,以应对细胞的新环境。这种改变后的行为依赖于外周肌动蛋白网络的重组。血小板就是这些过程的一个典型例子,目前关于细胞骨架功能的许多信息都来自血小板。在众多肌动蛋白交联蛋白中,如血影蛋白、丝束蛋白或α辅肌动蛋白,细丝蛋白A(FLNa)在三维肌动蛋白凝胶形成过程中启动肌动蛋白丝(F-肌动蛋白)聚合的潜力最大。FLNa还通过其C末端区域将肌动蛋白丝与血小板中许多膜糖蛋白的胞质结构域相连。除了参与细胞形态变化外,FLNa还是一种支架蛋白,可招募许多参与完全不同功能的蛋白质,包括信号转导、基因转录调控和受体转运;然而,FLNa在这些过程中的生理作用仍不清楚。本通讯的目的是简要描述能够与FLNa相互作用的大分子的特征,并讨论FLNa在血小板中这些分子元件的信号转导过程中可能发挥的作用。

相似文献

1
[Platelet filamin: a cytoskeletal protein involved in cell signal integration and function].血小板细丝蛋白:一种参与细胞信号整合与功能的细胞骨架蛋白
Arch Cardiol Mex. 2006 Oct-Dec;76 Suppl 4:S67-75.
2
[The filamin in cell signaling].[细胞信号传导中的细丝蛋白]
Tsitologiia. 2006;48(11):924-34.
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Filamin is essential in actin cytoskeletal assembly mediated by p21-activated kinase 1.细丝蛋白在由p21激活激酶1介导的肌动蛋白细胞骨架组装中至关重要。
Nat Cell Biol. 2002 Sep;4(9):681-90. doi: 10.1038/ncb838.
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Terminal differentiation of osteoblasts to osteocytes is accompanied by dramatic changes in the distribution of actin-binding proteins.成骨细胞向骨细胞的终末分化伴随着肌动蛋白结合蛋白分布的显著变化。
J Bone Miner Res. 2004 Mar;19(3):471-8. doi: 10.1359/JBMR.040128. Epub 2004 Jan 27.
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Cytoskeletal proteins and platelet signaling.细胞骨架蛋白与血小板信号传导
Thromb Haemost. 2001 Jul;86(1):198-213.
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Skeletal dysplasias due to filamin A mutations result from a gain-of-function mechanism distinct from allelic neurological disorders.由于细丝蛋白 A 突变导致的骨骼发育不良是一种不同于等位基因神经紊乱的获得性功能机制。
Hum Mol Genet. 2009 Dec 15;18(24):4791-800. doi: 10.1093/hmg/ddp442. Epub 2009 Sep 22.
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Intracellular factor XIII crosslinks platelet cytoskeletal elements upon platelet activation.细胞内因子 XIII 在血小板活化时交联血小板细胞骨架成分。
Thromb Haemost. 2002 Aug;88(2):315-20.
8
Filamin A mediates interactions between cytoskeletal proteins that control cell adhesion.细丝蛋白 A 介导细胞骨架蛋白之间的相互作用,这些蛋白控制细胞黏附。
FEBS Lett. 2011 Jan 3;585(1):18-22. doi: 10.1016/j.febslet.2010.11.033. Epub 2010 Nov 21.
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Structural determinants of LL5beta subcellular localisation and association with filamin C.LL5β亚细胞定位及与细丝蛋白C结合的结构决定因素
Cell Signal. 2007 Apr;19(4):817-24. doi: 10.1016/j.cellsig.2006.10.007. Epub 2006 Dec 14.
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Calcineurin dephosphorylates the C-terminal region of filamin in an important regulatory site: a possible mechanism for filamin mobilization and cell signaling.钙调神经磷酸酶使细丝蛋白的C末端区域在一个重要调控位点去磷酸化:细丝蛋白动员和细胞信号传导的一种可能机制。
Arch Biochem Biophys. 2006 Feb 15;446(2):140-50. doi: 10.1016/j.abb.2005.12.006. Epub 2005 Dec 29.

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