In Situ Synthesis and Visualization of Membrane SNAP25 Nano-Organization

Cryo-electron tomography (cryo-ET) can provide insights into the structure and states of natural membrane environments to explore the role of SNARE proteins at membrane fusion and understand the relationship between their subcellular localization/formation and action mechanism. Nevertheless, the identification of individual molecules in crowded and low signal-to-noise ratio membrane environments remains a significant challenge. In this study, cryo-ET is employed to image near-physiological state 293T cell membranes, specifically utilizing in situ synthesized gold nanoparticles (AuNPs) bound with cysteine-rich protein tags to single-molecularly labeled synaptosomal-associated protein 25 (SNAP25) on the membrane surface. The high-resolution images reveal that SNAP25 is predominantly located in regions of high molecular density within the cell membrane and aggregates into smaller clusters, which may increase the fusion efficiency. Remarkably, a zigzag arrangement of SNAP25 is observed on the cell membrane. These findings provide valuable insights into the functional mechanisms of SNARE proteins.

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Publication Details

Journal
Langmuir
Published
2024-09-27
DOI
https://doi.org/10.1021/acs.langmuir.4c02231
Citations
1
Primary Topic
Cellular transport and secretion
Type
article
Field-Weighted Citation Impact
0.33

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In Situ Synthesis and Visualization of Membrane SNAP25 Nano-Organization

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article

In Situ Synthesis and Visualization of Membrane SNAP25 Nano-Organization

Jinrui Zhang, Huili Wang, Yaxuan Zhang, Hongda Wang, Sihang Cheng
article en
1 citations

Abstract

Cryo-electron tomography (cryo-ET) can provide insights into the structure and states of natural membrane environments to explore the role of SNARE proteins at membrane fusion and understand the relationship between their subcellular localization/formation and action mechanism. Nevertheless, the identification of individual molecules in crowded and low signal-to-noise ratio membrane environments remains a significant challenge. In this study, cryo-ET is employed to image near-physiological state 293T cell membranes, specifically utilizing in situ synthesized gold nanoparticles (AuNPs) bound with cysteine-rich protein tags to single-molecularly labeled synaptosomal-associated protein 25 (SNAP25) on the membrane surface. The high-resolution images reveal that SNAP25 is predominantly located in regions of high molecular density within the cell membrane and aggregates into smaller clusters, which may increase the fusion efficiency. Remarkably, a zigzag arrangement of SNAP25 is observed on the cell membrane. These findings provide valuable insights into the functional mechanisms of SNARE proteins.

LangmuirVol. 40(40)
University of Science and Technology of China (CN), Chinese Academy of Sciences (CN), Changchun Institute of Applied Chemistry (CN), Qingdao National Laboratory for Marine Science and Technology (CN)
Natural Science Foundation of Jilin Province, National Natural Science Foundation of China, Chinese Academy of Sciences, Natural Science Foundation for Young Scientists of Shanxi Province, Guangdong Province Introduction of Innovative R&D Team
Openalex Percentile: Top 41%
Cellular transport and secretion
0.33
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