The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Cofilin is a pH sensor for actin free barbed end formation: role of phosphoinositide binding
Open accessAbstract
Newly generated actin free barbed ends at the front of motile cells provide sites for actin filament assembly driving membrane protrusion. Growth factors induce a rapid biphasic increase in actin free barbed ends, and we found both phases absent in fibroblasts lacking H+ efflux by the Na-H exchanger NHE1. The first phase is restored by expression of mutant cofilin-H133A but not unphosphorylated cofilin-S3A. Constant pH molecular dynamics simulations and nuclear magnetic resonance (NMR) reveal pH-sensitive structural changes in the cofilin C-terminal filamentous actin binding site dependent on His133. However, cofilin-H133A retains pH-sensitive changes in NMR spectra and severing activity in vitro, which suggests that it has a more complex behavior in cells. Cofilin activity is inhibited by phosphoinositide binding, and we found that phosphoinositide binding is pH-dependent for wild-type cofilin, with decreased binding at a higher pH. In contrast, phosphoinositide binding by cofilin-H133A is attenuated and pH insensitive. These data suggest a molecular mechanism whereby cofilin acts as a pH sensor to mediate a pH-dependent actin filament dynamics.
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Friesner, R. A., Banks, J. L., Murphy, R. B., Halgren, T. A., Klicic, J. J., Mainz, D. T., Repasky, M. P., Knoll, E. H., Shelley, M., Perry, J. K., et al. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm0306430 · Cited by 10,057
The Amber biomolecular simulation programs
Case, D. A., Cheatham, T. E., Darden, T., Gohlke, H., Luo, R., Merz, K. M., Onufriev, A., Simmerling, C., Wang, B., & Woods, R. J. (2005) · Journal of Computational Chemistry · doi:10.1002/jcc.20290 · Cited by 9,535
How is actin polymerization nucleated in vivo?
Condeelis, J. (2001) · Trends in Cell Biology · doi:10.1016/s0962-8924(01)02008-6 · Cited by 258
Self-citationEGF-induced PIP2 hydrolysis releases and activates cofilin locally in carcinoma cells
van Rheenen, J., Song, X., van Roosmalen, W., Cammer, M., Chen, X., DesMarais, V., Yip, S.-C., Backer, J. M., Eddy, R. J., & Condeelis, J. S. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200706206 · Cited by 244
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Random versus directionally persistent cell migration
Petrie, R. J., Doyle, A. D., & Yamada, K. M. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2729 · Cited by 954
Koivusalo, M., Welch, C., Hayashi, H., Scott, C. C., Kim, M., Alexander, T., Touret, N., Hahn, K. M., & Grinstein, S. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200908086 · Cited by 889
ADF/Cofilin: a functional node in cell biology
Bernstein, B. W., & Bamburg, J. R. (2010) · Trends in Cell Biology · doi:10.1016/j.tcb.2010.01.001 · Cited by 704
pH sensing and regulation in cancer
Damaghi, M., Wojtkowiak, J. W., & Gillies, R. J. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00370 · Cited by 536
Functions of cofilin in cell locomotion and invasion
Bravo-Cordero, J. J., Magalhaes, M. A. O., Eddy, R. J., Hodgson, L., & Condeelis, J. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3609 · Cited by 461
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Metadata
- Authors
- Frantz, C., Barreiro, G., Dominguez, L., Chen, X., Eddy, R., Condeelis, J., Kelly, M. J. S., Jacobson, M. P., & Barber, D. L.
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2008-11-24
- Volume
- 183
- Issue
- 5
- Pages
- 865-879
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2109493256
- Cited by
- 198
- References
- 4
- FWCI
- 5.12
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Frantz, C., Barreiro, G., Dominguez, L., Chen, X., Eddy, R., Condeelis, J., Kelly, M. J. S., Jacobson, M. P., & Barber, D. L. (2008). Cofilin is a pH sensor for actin free barbed end formation: role of phosphoinositide binding. The Journal of Cell Biology. https://doi.org/10.1083/jcb.200804161
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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