在老鼠视网膜中,Necl-1/CADM3调节了状突触的形成
Rumi Kawashima1, Kenji Matsushita1, Kenji Mandai2,3,4
1Department of Ophthalmology, Osaka University Graduate School of Medicine, Suita, Osaka 565-0871, Japan.
iScience
|April 16, 2024
概括
Necl-1蛋白对于在小鼠视网膜中形成突触至关重要,确保短波长光的正确视觉信号传输. 它的缺失会破坏这些连接,损害视力.
科学领域:
- 神经科学是一个神经科学.
- 视网膜生物学 视网膜生物学
- 突触性可塑性 突触性可塑性
背景情况:
- 外状层是脊椎动物视觉处理中的初始突触部位.
- 对于OFF通路的突触形成的分子机制尚未完全理解.
研究的目的:
- 研究Necl-1/CADM3在突触形成和功能中的作用.
- 为了阐明由短波长光介导的OFF通路的分子调节.
主要方法:
- 免疫组织化学测定Necl-1/CADM3在视网膜细胞中的定位.
- 在Necl-1淘汰赛小鼠中分析圆双极细胞 (CBC) 突触形成和受体分布.
- 电生理学记录,以评估从体到OFF CBC的信号传输.
- 在Necl-1缺乏的小鼠中评估光动力学反应.
主要成果:
- 尼克尔-1/CADM3局限于体和4型OFF CBC树突.
- Necl-1 缺乏导致-CBC 突触的脱,异常的水平细胞分布,AMPA 受体的错位.
- 在Necl-1淘汰赛小鼠中,短波光信号传输到OFF CBC受损.
- AMPA受体的强化挽救了异常信号传输.
- Necl-1 淘汰赛小鼠在光动力学反应中表现出缺陷.
结论:
- 在哺乳动物视网膜中,Necl-1对于适当的突触形成至关重要.
- Necl-1 调节了用于短波长光感知的 OFF 圆通路.
- 破坏Necl-1功能会导致视觉处理缺陷.
相关概念视频
Notch Signaling Pathway
4.6K
The Notch signaling pathway is a major intracellular signaling pathway that is highly conserved over a broad spectrum of metazoan species. It stands unique from other intracellular signaling mechanisms in animals because notch protein itself acts as the receptor as well as the primary signaling molecule.
The Notch gene came into the limelight in 1914 after the discovery that its mutation in Drosophila melanogaster leads to a serrated (or "notched") wing margin phenotype. It was not...
The Notch gene came into the limelight in 1914 after the discovery that its mutation in Drosophila melanogaster leads to a serrated (or "notched") wing margin phenotype. It was not...
4.6K
Mechanism of Lamellipodia Formation
3.1K
Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
3.1K
Intracellular Signaling Affects Focal Adhesions
2.8K
Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Some...
2.8K
Structure of Cadherins
4.0K
The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins” is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This...
4.0K
Catenins
2.2K
Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the...
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the...
2.2K
Immunoglobulin-like Cell Adhesion Molecules
3.3K
Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
3.3K


