通过Ena/VASP蛋白质对纤维细胞运动的负调节
J E Bear1, J J Loureiro, I Libova
1Department of Biology, Massachusetts Institute of Technology, Cambridge, USA.
Cell
|July 13, 2000
概括
发现对细胞运动至关重要的Ena/VASP蛋白质阻碍了纤维细胞运动. 它们的去除增加了细胞运动,挑战了Ena/VASP功能的现有模型.
科学领域:
- 细胞生物学 细胞生物学
- 分子生物学分子生物学
- 生物化学 生物化学
背景情况:
- 埃纳/VASP蛋白质通过调节行动蛋白细胞骨架,参与细胞运动.
- 它们通常在焦点粘附处和细胞的前沿发现.
研究的目的:
- 研究Ena/VASP蛋白在纤维细胞运动中的作用.
- 为了确定Ena/VASP蛋白是否积极或消极地调节细胞运动.
主要方法:
- 纤维细胞中Ena/VASP蛋白的过度表达.
- 功能丧失研究涉及中和或删除Ena/VASP蛋白质.
- 将Ena/VASP蛋白向细胞膜.
主要成果:
- 过度表达Ena/VASP蛋白导致纤维细胞运动的剂量依赖性下降.
- 完全去除或中和Ena/VASP蛋白导致细胞运动的增强.
- 从焦点粘附中削减Ena/VASP蛋白质不会影响运动性,但构成性膜向抑制了它.
结论:
- 埃纳/VASP蛋白质对纤维细胞运动有负面调节,这与一些既有模型相反.
- Ena/VASP蛋白的定位对于它们在细胞运动中的功能至关重要.
- 这些发现与基于Listeria monocytogenes基于actin的移动性的模型形成对比.
相关概念视频
Mechanical Protein Functions
Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force.
Generation of Straight or Branched Actin Filaments
The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
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...
In F-actin, the ADF/cofilin proteins...
Cell-matrix's Response to Mechanical Forces
In animal cells, the extracellular matrix allows cells within tissues to withstand external stresses and transmits signals from the outside of the cell to the inside. The extracellular matrix is extensive, and its composition varies between different types of tissues. For example, the reticular fibers and ground substance make up the ECM in loose connective tissue, while collagen and bone minerals make up the ECM of bone tissue.
Anchoring junctions mechanically attach a cell to the...
Anchoring junctions mechanically attach a cell to the...
Protein Dynamics in Living Cells
Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
Tension Response at Adherens Junctions
The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin homology) domains...
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin homology) domains...


