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相关概念视频

Fusion of Secretory Vesicles with the Plasma Membrane01:26

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Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
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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.
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Pinching-off of Coated Vesicles01:32

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Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
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Vesicular Tubular Clusters01:45

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After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
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Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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In Vivo Single-Molecule Tracking at the Drosophila Presynaptic Motor Nerve Terminal
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赛纳普托塔格明7对接突触囊泡,以支持促进和Doc2α触发的异步释放.

Zhenyong Wu1,2, Grant F Kusick3,4, Manon M M Berns5

  • 1Department of Neuroscience, University of Wisconsin-Madison, Madison, United States.

eLife
|March 27, 2024
PubMed
概括

Doc2α是异步神经递质释放的主要传感器,而synaptotagmin 7 (syt7) 则有助于突触囊泡对接. 这阐明了激发性突触中异步释放的分子机制.

关键词:
异步释放是一种异步释放.细胞生物学 细胞生物学iGluSnFR 的使用情况.这里是鼠标鼠标鼠标鼠标鼠标鼠标.神经科学 神经科学短期的可塑性是短期的可塑性.突触囊泡的对接方式这是一种突触突触 (synaptotagmin).这是一个zap-and-freeze系统.

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科学领域:

  • 神经科学是一个神经科学.
  • 分子生物学分子生物学
  • 细胞生物学 细胞生物学

背景情况:

  • 不同步神经递质释放背后的分子机制尚未完全理解.
  • 突触胺 (syt) 7和Doc2已被认为是该过程中的传感器,但它们的具体作用仍在争论中.

研究的目的:

  • 阐明Doc2α和syt7在刺激性小鼠海马突触中的异步神经递质释放中的不同作用.
  • 为了解决围绕传感器负责异步异细胞形成的争议.

主要方法:

  • 在小鼠海马神经元中利用了Doc2α和syt7的遗传删除 (Knockout).
  • 评估神经递质释放动力学,包括同步和异步释放,使用电生理学记录.
  • 研究了突触囊泡对接和补充动态.

主要成果:

  • Doc2α是异步释放的主要Ca2+传感器;它的缺失大大减少了单动电位后的释放.
  • Syt7对于突触囊泡的活动依赖性对接至关重要,确保在重复活动期间持续释放的补充.
  • 破坏Doc2α和syt7都显示出非添加效应,支持它们的不同作用.

结论:

  • Doc2α作为主要的Ca2+传感器,用于异步的神经递质释放.
  • Syt7通过促进活动依赖的突触囊泡对接来促进异步释放.
  • 一个新的模型提出syt7驱动器对接,为同步 (syt1-介导) 和异步 (Doc2α和其他传感器) 释放提供囊泡.