The DOI matches its Crossref record; 50 of the 50 references it cites were found in a registry or an index.
VASP is a processive actin polymerase that requires monomeric actin for barbed end association
Open accessAbstract
Ena/VASP proteins regulate the actin cytoskeleton during cell migration and morphogenesis and promote assembly of both filopodial and lamellipodial actin networks. To understand the molecular mechanisms underlying their cellular functions we used total internal reflection fluorescence microscopy to visualize VASP tetramers interacting with static and growing actin filaments in vitro. We observed multiple filament binding modes: (1) static side binding, (2) side binding with one-dimensional diffusion, and (3) processive barbed end tracking. Actin monomers antagonize side binding but promote high affinity (Kd = 9 nM) barbed end attachment. In low ionic strength buffers, VASP tetramers are weakly processive (Koff = 0.69 s−1) polymerases that deliver multiple actin monomers per barbed end–binding event and effectively antagonize filament capping. In higher ionic strength buffers, VASP requires profilin for effective polymerase and anti-capping activity. Based on our observations, we propose a mechanism that accounts for all three binding modes and provides a model for how VASP promotes actin filament assembly.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Cellular Motility Driven by Assembly and Disassembly of Actin Filaments
Pollard, T. D., & Borisy, G. G. (2003) · Cell · doi:10.1016/s0092-8674(03)00120-x · Cited by 4,195
Cell mechanics and the cytoskeleton
Fletcher, D. A., & Mullins, R. D. (2010) · Nature · doi:10.1038/nature08908 · Cited by 2,989
Self-citationAntagonism between Ena/VASP Proteins and Actin Filament Capping Regulates Fibroblast Motility
Bear, J. E., Svitkina, T. M., Krause, M., Schafer, D. A., Loureiro, J. J., Strasser, G. A., Maly, I. V., Chaga, O. Y., Cooper, J. A., Borisy, G. G., et al. (2002) · Cell · doi:10.1016/s0092-8674(02)00731-6 · Cited by 847
Aitken, C. E., Marshall, R. A., & Puglisi, J. D. (2008) · Biophysical Journal · doi:10.1529/biophysj.107.117689 · Cited by 843
Mechanism of filopodia initiation by reorganization of a dendritic network
Svitkina, T. M., Bulanova, E. A., Chaga, O. Y., Vignjevic, D. M., Kojima, S.-I., Vasiliev, J. M., & Borisy, G. G. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200210174 · Cited by 770
Nonblinking and long-lasting single-molecule fluorescence imaging
Rasnik, I., McKinney, S. A., & Ha, T. (2006) · Nature Methods · doi:10.1038/nmeth934 · Cited by 702
Gertler, F. B., Niebuhr, K., Reinhard, M., Wehland, J., & Soriano, P. (1996) · Cell · doi:10.1016/s0092-8674(00)81341-0 · Cited by 663
Control of the Assembly of ATP- and ADP-Actin by Formins and Profilin
Kovar, D. R., Harris, E. S., Mahaffy, R., Higgs, H. N., & Pollard, T. D. (2006) · Cell · doi:10.1016/j.cell.2005.11.038 · Cited by 562
Cellular Control of Actin Nucleation
Welch, M. D., & Mullins, R. D. (2002) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.18.040202.112133 · Cited by 517
Self-citationRole of fascin in filopodial protrusion
Vignjevic, D., Kojima, S.-I., Aratyn, Y., Danciu, O., Svitkina, T., & Borisy, G. G. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200603013 · Cited by 484
Cited by
Actin Dynamics, Architecture, and Mechanics in Cell Motility
Blanchoin, L., Boujemaa-Paterski, R., Sykes, C., & Plastino, J. (2014) · Physiological Reviews · doi:10.1152/physrev.00018.2013 · Cited by 1,457
Ridley, A. J. (2011) · Cell · doi:10.1016/j.cell.2011.06.010 · Cited by 956
Actin and Actin-Binding Proteins
Pollard, T. D. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a018226 · Cited by 912
Calcineurin Orchestrates Lateral Transfer of Aspergillus fumigatus during Macrophage Cell Death
Shah, A., Kannambath, S., Herbst, S., Rogers, A., Soresi, S., Carby, M., Reed, A., Mostowy, S., Fisher, M. C., Shaunak, S., et al. (2016) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201601-0070oc · Cited by 71
Actin dynamics associated with focal adhesions
Ciobanasu, C., Faivre, B., & Le Clainche, C. (2012) · International Journal of Cell Biology · doi:10.1155/2012/941292 · Cited by 63
Metadata
- Authors
- Hansen, S. D., & Mullins, R. D.
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2010-11-01
- Volume
- 191
- Issue
- 3
- Pages
- 571-584
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W1987338177
- Cited by
- 271
- References
- 50
- FWCI
- 8.23
- Type
- journal article
- Language
- en
- Open access
- hybrid
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: VASP is a processive actin polymerase that requires monomeric actin for barbed end association. https://app.cochat.ai/papers/10.1083/jcb.201003014
- The paper
- Hansen, S. D., & Mullins, R. D. (2010). VASP is a processive actin polymerase that requires monomeric actin for barbed end association. Journal of Cell Biology. https://doi.org/10.1083/jcb.201003014
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
