亨廷丁纤维刺伤膜
Pedro Guedes-Dias1, Erika L F Holzbaur1
1Department of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104-6085, USA.
Cell
|September 23, 2017
概括
亨廷顿病聚合物具有与内质网相互作用的纤维结构. 这种相互作用扭曲了内质网的形状和功能,为疾病提供了新的见解.
科学领域:
- 神经科学
- 细胞生物学
- 生物化学
背景情况:
- 亨廷顿病的特征是细胞内突变的亨廷.
- 这些聚合物的病理作用一直是现场的一个长期问题.
研究的目的:
- 为了阐明突变的亨廷丁聚合物的现场结构.
- 研究亨廷丁聚合物与细胞器官之间的相互作用,特别是内质网膜.
主要方法:
- 使用冷电子断层扫描以高分辨率可视化聚合物.
- 在细胞内对huntingtin聚合物的实地结构分析.
主要成果:
- 这项研究揭示了猎聚合物的纤维性.
- 观察到亨廷丁纤维素与内质网直接相互作用.
- 这种相互作用导致了可观察到的内等质网形态和动态变化.
结论:
- 突变的亨廷丁聚合物具有明确的纤维结构.
- 这些纤维与内质网的相互作用导致亨廷顿病的细胞功能障碍.
- 这些发现提供了聚合物形成与内质网膜病理之间的机制联系.
相关概念视频
SNAREs and Membrane Fusion
13.0K
Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
13.0K
Amyloid Fibrils
12.1K
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
12.1K
Formation of Intermediate Filaments
4.0K
Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been...
4.0K
The Structure of Intermediate Filaments
5.9K
The intermediate filaments are one of three widely studied cytoskeletal filaments. They are so named as their diameter (10 nm) is in between that of microfilaments (7 nm) and the microtubules (25 nm). These filaments are highly stable and can remain intact when exposed to high salt concentrations and detergents. These filaments are responsible for providing stability and mechanical support to the cells. They also help in cell adhesion and maintaining tissue integrity.
Intermediate...
Intermediate...
5.9K
Disassembly of Intermediate Filaments
2.7K
Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
2.7K
Assembly of Cytoskeletal Filaments
28.0K
Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
28.0K


