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Single-molecule fluorescence resonance energy transfer reveals a dynamic equilibrium between closed and open conformations of syntaxin 1
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Protein conformational transitions form the molecular basis of many cellular processes, such as signal transduction and membrane traffic. However, in many cases, little is known about their structural dynamics. Here we have used dynamic single-molecule fluorescence to study at high time resolution, conformational transitions of syntaxin 1, a soluble N -ethylmaleimide-sensitive factor attachment protein receptors protein essential for exocytotic membrane fusion. Sets of syntaxin double mutants were randomly labeled with a mix of donor and acceptor dye and their fluorescence resonance energy transfer was measured. For each set, all fluorescence information was recorded simultaneously with high time resolution, providing detailed information on distances and dynamics that were used to create structural models. We found that free syntaxin switches between an inactive closed and an active open configuration with a relaxation time of 0.8 ms, explaining why regulatory proteins are needed to arrest the protein in one conformational state.
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“Since the Förster radius for this pair is ∼6 nm (46) and energy transfer efficiency at longer distances drops precipitously, the data suggest that all three acceptor-labeled monomers (K18, 3R MAP2, and 4R MAP2) had added to the fibril end as schematically shown for K18 in the inset of Figure 5A.”
From MAP2 caps tau fibrils and inhibits aggregation (2023) · cites this paper as [46]
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Liu, Y., Pan, T., Wang, K., Wang, Y., Yan, S., Wang, L., Zhang, S., Du, X., Jia, W., Zhang, P., et al. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202110545 · Cited by 51
Price, E. S., DeVore, M. S., & Johnson, C. K. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp912125z · Cited by 51
Metadata
- Authors
- Margittai, M., Widengren, J., Schweinberger, E., Schröder, G. F., Felekyan, S., Haustein, E., König, M., Fasshauer, D., Grubmüller, H., Jahn, R., & Seidel, C. A. M.
- Affiliations
- Max Planck Institute for Biophysical Chemistry (DE)
- Max Planck Society (DE)
- Max-Planck-Institut für Biophysikalische Chemie, Am Fassberg 11, 37077 Göttingen, Germany
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2003-12-10
- Volume
- 100
- Issue
- 26
- Pages
- 15516-15521
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC307599
- OpenAlex
- W2128978059
- Cited by
- 290
- References
- 36
- Citations by year
- 2026: 1 · 2024: 5 · 2023: 9 · 2022: 9 · 2021: 11 · 2020: 3 · 2019: 9 · 2018: 5 · 2017: 10 · 2016: 9 · 2015: 13 · 2014: 10 · 2013: 12 · 2012: 23
- FWCI
- 7.43
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- GRO (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion, other-oa)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Advanced Fluorescence Microscopy Techniques
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- syntaxin-1, conformational dynamics, SNARE proteins, exocytosis, membrane fusion, single-molecule fluorescence resonance energy transfer, protein structural dynamics
- MeSH terms
- Antigens, Surface, Cysteine, Kinetics, Models, Molecular, Nerve Tissue Proteins, Protein Conformation, Recombinant Proteins, Serine, Mutagenesis, Site-Directed, Amino Acid Substitution, Fluorescence Resonance Energy Transfer, Syntaxin 1
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