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相关概念视频

Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

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...
SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

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...
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
Rab Cascades01:25

Rab Cascades

Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.

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相关实验视频

Updated: Jul 8, 2026

Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay
09:19

Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay

Published on: October 19, 2012

细胞内膜t-SNARE的功能架构

R Fukuda1, J A McNew, T Weber

  • 1Cellular Biochemistry & Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA.

Nature
|September 23, 2000
PubMed
概括
此摘要是机器生成的。

细胞内目标膜SNAREs (t-SNAREs) 使用单独的光链,而不是合的SNAP-25蛋白. 这一发现表明SNAP-25是SNAP-25.

更多相关视频

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy
10:58

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy

Published on: August 24, 2016

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
08:55

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy

Published on: December 29, 2017

相关实验视频

Last Updated: Jul 8, 2026

Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay
09:19

Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay

Published on: October 19, 2012

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy
10:58

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy

Published on: August 24, 2016

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
08:55

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy

Published on: December 29, 2017

科学领域:

  • 分子生物学分子生物学
  • 细胞生物学 细胞生物学
  • 生物化学 生物化学

背景情况:

  • 脂质双层融合对细胞过程至关重要,由SNARE蛋白质进行介导.
  • 溶性N-乙基胺敏感因子附着蛋白受体 (SNAREs) 组装成一个四螺旋束,囊泡SNAREs (v-SNAREs) 提供一个螺旋和目标SNAREs (t-SNAREs) 提供三个螺旋.
  • 血t-SNAREs通常由合成素和来自SNAP-25.5的两个螺旋体组成.

研究的目的:

  • 为了研究t-SNAREs在细胞内膜上的组成.
  • 为了确定在细胞内t-SNARE复合体中取代SNAP-25的组件.
  • 了解SNARE蛋白质结构的进化分歧.

主要方法:

  • 在不同细胞区间对SNARE蛋白质同类的比较分析.
  • 细胞内t-SNARE复合体的结构和功能表征.
  • 基因进化和蛋白质域融合的生物信息分析.

主要成果:

  • 细胞内t-SNAREs由一种合成素同类的"重链"和两个不同的非合成素"轻链"组成.
  • 与等离子膜t-SNAREs不同,细胞内t-SNAREs在其三个螺旋体中不使用同类于SNAP-25的单一蛋白质.
  • 酵母Sec9和Spo20,虽然与SNAP-25相关,但局部存在于血膜中,并且似乎不能替代细胞内SNAP-25的功能.

结论:

  • 细胞内t-SNAREs的结构与血t-SNAREs的结构有很大的不同,它们使用单独的光链,而不是融合的SNAP-25.
  • SNAP-25可能代表了一个进化上的例外,可能来自于编码单独光链的基因的融合.
  • 这项研究阐明了SNARE复合物的分子多样性及其对膜贩运通路的影响.