Cited by 523Cellular Mechanics and InteractionsProtein Kinase Regulation and GTPase SignalingMicrotubule and mitosis dynamics

Latrunculin alters the actin-monomer subunit interface to prevent polymerization

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Morton, Walter M., Ayscough, Kathryn R., McLaughlin, Paul J.·2000·Nature Cell Biology

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Crossref · 10.1038/35014075

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  • Latrunculin A treatment completely blocks ultrafast endocytosis, with no induction of membrane pit formation.

    “When neurons are treated with Latrunculin A, which sequesters monomeric actin (G-actin) and perturbs F-actin formation12,13, ultrafast endocytosis fails completely, with no induction of membrane pit formation5.”

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Authors
Morton, W. M., Ayscough, K. R., & McLaughlin, P. J.
Affiliations
  • Wellcome Centre for Cell Biology (GB)
  • University of Glasgow (GB)
Corresponding author
McLaughlin, Paul J.
Venue
Nature Cell Biology
Published
2000-05-12
Volume
2
Issue
6
Pages
376-378
ISSN
  • 1465-7392 (ISSN-L)
  • 1476-4679
OpenAlex
W1545247886
Cited by
523
References
1
Citations by year
2026: 11 · 2025: 19 · 2024: 20 · 2023: 18 · 2022: 25 · 2021: 22 · 2020: 24 · 2019: 21 · 2018: 23 · 2017: 11 · 2016: 21 · 2015: 25 · 2014: 20 · 2013: 26 · 2012: 16
FWCI
6.18
Type
journal article
Language
en
Open access
Locations
  • Nature Cell Biology (publishedVersion)
  • PubMed (publishedVersion)
  • ERA (submittedVersion)
  • Science and Technology Facilities Council (submittedVersion)
Funders
  • Wellcome Trust (050934)
  • European Commission
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Keywords
latrunculin, actin, actin polymerization, actin filament structure, actin-binding proteins, actin cytoskeleton
MeSH terms
Actins, Animals, Binding Sites, Biopolymers, Humans, Models, Molecular, Molecular Sequence Data, Mutation, Porifera, Protein Binding, Protein Conformation, Thiazoles, Yeasts, Gelsolin, Crystallography, X-Ray, Bridged Bicyclo Compounds, Heterocyclic, Thiazolidines

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