Effects of cytochalasin and phalloidin on actin.

Cooper, J A

doi:10.1083/jcb.105.4.1473

Cited by 2,009Cellular Mechanics and InteractionsMicrotubule and mitosis dynamicsProtein Structure and Dynamics

Effects of cytochalasin and phalloidin on actin.

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Cooper, J A·1987·The Journal of cell biology

DOI 10.1083/jcb.105.4.1473PMC PMC2114638

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At low concentrations, cytochalasins primarily cap the barbed ends of actin filaments.
“at low concentrations, their primary effect in cells is to cap the barbed ends of actin filaments (3).”
From Dynamic actin filaments are required for stable long-term potentiation (LTP) in area CA1 of the hippocampus (2000) · cites this paper as [3]
Low concentrations of AAIs (0.01-1 μM) are similar to those shown previously to alter actin filament organization in cultured cells, prevent lamellipodial ruffling in fibroblasts, inhibit motility and retrograde flow in neuronal growth cones, and arrest dendritic spine motility in hippocampal neurons.
“The concentrations of latrunculin A and cytochalasins used here (0.01–1 μM) are similar to those that have been shown previously to alter actin filament organization in cultured cells, prevent lamellipodial ruffling in fibroblasts, inhibit motility and retrograde flow in neuronal growth cones, and arrest dendritic spine motility in hippocampal neurons (3, 4, 7, 10).”
From Dynamic actin filaments are required for stable long-term potentiation (LTP) in area CA1 of the hippocampus (2000) · cites this paper as [3]

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Authors: Cooper, J. A.
Affiliations: Washington University in St. Louis (US)
Corresponding author: Cooper, J A
ORCID: Cooper, J A
Venue: The Journal of cell biology
Publisher: Rockefeller University Press
Published: 1987-10-01
Volume: 105
Issue: 4
Pages: 1473-1478
ISSN: 0021-9525 (ISSN-L)
1540-8140
DOI: 10.1083/jcb.105.4.1473
PMC: PMC2114638
OpenAlex: W2119632652
Cited by: 2,009
References: 56
Citations by year: 2026: 28 · 2025: 33 · 2024: 23 · 2023: 27 · 2022: 37 · 2021: 42 · 2020: 51 · 2019: 40 · 2018: 60 · 2017: 51 · 2016: 41 · 2015: 52 · 2014: 58 · 2013: 42 · 2012: 57
FWCI: 15.79
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: cc-by-nc-sa
Locations: The Journal of Cell Biology (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
PubMed Central (publishedVersion, cc-by-nc-sa)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords: cytochalasin, phalloidin, actin, actin polymerization, actin depolymerization, actin-binding proteins
MeSH terms: Actins, Animals, Cell Movement, Cytochalasins, Cytoskeleton, Humans, Actin Cytoskeleton, Oligopeptides, Phalloidine, In Vitro Techniques

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