Cysteine-rich protein 2 accelerates actin filament cluster formation.

Cysteine-rich protein 2 accelerates actin filament cluster formation.
复制标题

DOI:
10.1371/journal.pone.0183085
复制
发表时间:
2017
期刊:
影响因子:
3.7
通讯作者:
Miyake J
Miyake J
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Kihara T;Sugimoto Y;Shinohara S;Takaoka S;Miyake J

文献摘要

参考文献

被引文献

相似文献

丝状肌动蛋白(F-actin)形成多种结构,动态调节细胞形态和运动,对细胞外刺激起机械感觉作用。在这项研究中,我们确定了与平滑肌相关的转录因子半胱氨酸丰富蛋白2(CRP2)调节F-肌动蛋白的超分子网络。用小角X射线溶液散射(SAXS)分析CRP2和F-肌动蛋白在溶液中的结构。CRP2的总体形状是部分展开的,结构上相对椭圆形,其表观回转横截面半径(RC)约为15.8ä。通过从头算模拟得出的预测形状,大约由四个串联簇组成:LIM结构域可能在两端,中间簇是一个未折叠的连接区。SAXS分析表明,F-肌动蛋白的Rc约为26.7ä,与CRP2的加入量无关。另一方面,在CRP2结合的F-肌动蛋白散射的低角度区域,随着CRP2的加入,其强度呈现上曲,这表明在CRP2结合后,F-肌动蛋白的分支增加。从生化分析来看,CRP2的加入使肌动蛋白细丝增大并聚集在一起。CRP2的这种F-肌动蛋白聚集活性与α-肌动蛋白协同作用。因此,CRP2与F-肌动蛋白的结合加速了肌动蛋白聚合和F-肌动蛋白簇的形成。
Filamentous actin (F-actin) forms many types of structures and dynamically regulates cell morphology and movement, and plays a mechanosensory role for extracellular stimuli. In this study, we determined that the smooth muscle-related transcription factor, cysteine-rich protein 2 (CRP2), regulates the supramolecular networks of F-actin. The structures of CRP2 and F-actin in solution were analyzed by small-angle X-ray solution scattering (SAXS). The general shape of CRP2 was partially unfolded and relatively ellipsoidal in structure, and the apparent cross sectional radius of gyration (Rc) was about 15.8 Å. The predicted shape, derived by ab initio modeling, consisted of roughly four tandem clusters: LIM domains were likely at both ends with the middle clusters being an unfolded linker region. From the SAXS analysis, the Rc of F-actin was about 26.7 Å, and it was independent of CRP2 addition. On the other hand, in the low angle region of the CRP2-bound F-actin scattering, the intensities showed upward curvature with the addition of CRP2, which indicates increasing branching of F-actin following CRP2 binding. From biochemical analysis, the actin filaments were augmented and clustered by the addition of CRP2. This F-actin clustering activity of CRP2 was cooperative with α-actinin. Thus, binding of CRP2 to F-actin accelerates actin polymerization and F-actin cluster formation.
DOI: 10.1016/0092-8674(94)90192-9
发表时间: 1994-10-21
期刊: CELL
影响因子: 64.5
作者:
ARBER, S;HALDER, G;CARONI, P
通讯作者: CARONI, P
DOI: 10.1074/jbc.273.36.23233
发表时间: 1998-09-04
影响因子: 4.8
作者:
Konrat, R;Kräutler, B;Bister, K
通讯作者: Bister, K
DOI: 10.1038/nature09372
发表时间: 2010-10-07
期刊: NATURE
影响因子: 64.8
作者:
Fujii, Takashi;Iwane, Atsuko H.;Namba, Keiichi
通讯作者: Namba, Keiichi
DOI: 10.18632/oncotarget.7327
发表时间: 2016-03-22
期刊: Oncotarget
影响因子: --
作者:
Hoffmann C;Mao X;Dieterle M;Moreau F;Al Absi A;Steinmetz A;Oudin A;Berchem G;Janji B;Thomas C
通讯作者: Thomas C
DOI: 10.1074/jbc.270.19.11437
发表时间: 1995-05-12
影响因子: 4.8
作者:
ISAMBERT, H;VENIER, P;CARLIER, MF
通讯作者: CARLIER, MF