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関連する概念動画

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...
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...
ATP Synthase: Structure01:18

ATP Synthase: Structure

ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
Tagging and Fusion Proteins01:24

Tagging and Fusion Proteins

Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
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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関連する実験動画

Updated: Jul 15, 2026

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

シナプトタグミンが膜融合を促進する方法

Sascha Martens1, Michael M Kozlov, Harvey T McMahon

  • 1Medical Research Council-Laboratory of Molecular Biology, Hills Road, CB2 0QH Cambridge, UK.

Science (New York, N.Y.)
|May 5, 2007
PubMed
まとめ

カルシウムセンサーであるシナプトタグミン-1は,膜融合のためのエネルギーバリアを下げる. それは,カルシウム結合時に膜の曲線を誘導することによって,SNARE媒介の膀エクソサイトーシスを促進します.

科学分野:

  • 分子生物学は分子生物学である.
  • 神経科学は神経科学である.
  • バイオフィジックス 生物物理学

背景:

  • 神経伝達物質の放出は,溶性N-エチルマレイミド感受因子結合タンパク質受容体 (SNARE) タンパク質によって調節されるプロセスであるシナプス膀エクソサイトーシスに依存する.
  • 急速なカルシウムイオン (Ca2+) の流入はエクソサイトーシスを誘発し,シナプトタグミン-1は急速な膀融合のための重要なCa2+センサーとして特定されています.
  • 膜融合,特に2層融合は,実質的な活性化エネルギーバリア (約. 40 k ((B) T).) である.

研究 の 目的:

  • シナプトタグミン-1がSNARE媒介の膜融合を促進するメカニズムを解明する.
  • シナプトタグミン-1が膀融合のための高活性化エネルギー障壁を克服する方法を調査する.

主な方法:

  • 膜相互作用と融合におけるシナプトタグミン-1のC2ドメインの役割を調査した.
  • シナプトタグミン-1へのCa2+結合が膜の曲線とSNARE複合体の機能に及ぼす生体物理学的効果を分析した.

主要な成果:

  • シナプトタグミン-1へのCa2+結合は,C2-ドメインの挿入によって標的膜の高正曲線を誘導する.
  • この誘導された膜の曲線は,二重層-二重層融合の活性化エネルギーを大幅に低下させます.

さらに関連する動画

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

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

関連する実験動画

Last Updated: Jul 15, 2026

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

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

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

  • シナプトタグミン-1は,Ca2+依存性プラズマ膜屈折とSNARE複合ジッパーリングを通じてドッキングされた膀融合を誘発する.

    • 結論:

    • シナプトタグミン-1は,エネルギー環境を積極的に削減することによって,膜融合の重要な調節剤として作用します.
    • このメカニズムには,Ca2+によって引き起こされる膜変形が関与し,SNARE駆動による融合を容易にします.
    • このCa2+依存の膜屈折とSNAREジッパーメカニズムは,膜融合イベントの保存された経路を表している可能性があります.