相关实验视频

Updated: Jan 23, 2026

Measuring Protein Binding to F-actin by Co-sedimentation

Measuring Protein Binding to F-actin by Co-sedimentation

Published on: May 18, 2017

SH3BGRL蛋白质是含有乙烯丝尖端封闭蛋白质 (TPECs) 的铁素折叠

Robin S Heiringhoff¹, Daniel Marke¹, Ute Curth¹

¹Institute for Biophysical Chemistry, Hannover Medical School, Fritz-Hartmann-Centre for Medical Research, Hannover, 30625, Germany.

Scientific reports

|January 21, 2026

概括

SH3BGRL蛋白质,现在被称为硫素折叠含有尖端封闭蛋白质 (TPECs),非酶性调节actin动态. 它们增强了动氨酸核和帽子丝末端,与热粒素合作调节脱聚合.

科学领域:

细胞生物学细胞生物学
生物化学生物化学
结构生物学是结构生物学.

背景情况:

动氨酸的动态对于细胞过程至关重要.
动氨酸结合蛋白通过专门的域调节这些动态.
SH3BGRL蛋白质具有硫素 (Trx) 折叠,但缺乏正规的酶体位点.

研究的目的:

为了研究SH3BGRL蛋白在调节细胞活性动态中的作用.
描述SH3BGRL蛋白中的Trx折叠的非酶功能.
为SH3BGRL蛋白家族提出一个新的功能分类.

主要方法:

在实验室内进行actin聚合试验.
分子动力学模拟.分子动力学模拟.
尖端的行为丝试验. 尖端的行为丝试验.
生物化学相互作用研究.

主要成果:

通过稳定actin二元和三元,SH3BGRL蛋白在很弱的程度上促进了actin核化.
这些蛋白质通过与终端子单元的直接关联来抑制尖端的活性子单元的添加.
SH3BGRL蛋白与热粒素合作,以异构体特定的方式增强尖端脱聚合抑制.
所有的异构体形成一个与actin和tropomodulin的三方复合体.

结论:

SH3BGRL蛋白质的非酶功能是调节actin动态.
它们充当尖端封闭蛋白质,影响核和脱聚合.
这一蛋白质家族在功能上被重新定义为含有硫素折叠的尖端封闭蛋白 (TPECs).

关键词:

动因动态的动力学动氨酸结合蛋白的蛋白质.封闭蛋白质是封闭蛋白质的组成部分.提奥雷多克辛可以折叠.

更多相关视频

Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin

Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin

Published on: March 28, 2008

Quantification of Filamentous Actin F-actin Puncta in Rat Cortical Neurons

Quantification of Filamentous Actin F-actin Puncta in Rat Cortical Neurons

Published on: February 10, 2016

相关概念视频

Protein Folding

Protein Folding

Protein Folding

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

Molecular Chaperones and Protein Folding

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...

Molecular Chaperones and Protein Folding

Molecular Chaperones and Protein Folding

Actin Filament Depolymerization

Actin Filament Depolymerization

Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...

Formation of Higher-order Actin Filaments

Formation of Higher-order Actin Filaments

The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin...