Ins and outs of ADF/cofilin activity and regulation
Abstract
The actin-binding proteins of the actin-depolymerisation factor (ADF)/cofilin family were first described more than three decades ago, but research on these proteins still occupies a front role in the actin and cell migration field. Moreover, cofilin activity is implicated in the malignant, invasive properties of cancer cells. The effects of ADF/cofilins on actin dynamics are diverse and their regulation is complex. In stimulated cells, multiple signalling pathways can be initiated resulting in different activation/deactivation switches that control ADF/cofilin activity. The output of this entire regulatory system, in combination with spatial and temporal segregation of the activation mechanisms, underlies the contribution of ADF/cofilins to various cell migration/invasion phenotypes. In this framework, we describe current views on how ADF/cofilins function in migrating and invading cells.
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Phosphorylation of cofilin at serine-3 inhibits its actin-regulatory activities, and phosphorylated cofilin dissociates from F-actin.
“These bidirectional enzymatic activities of cofilin are inhibited by its phosphorylation at the serine-3 residue, as phosphorylated cofilin (p-cofilin) dissociates from F-actin1516.”
From State-dependent diffusion of actin-depolymerizing factor/cofilin underlies the enlargement and shrinkage of dendritic spines (2016) · cites this paper as [15]
Dephosphorylated cofilin at serine-3 cleaves F-actin to generate new barbed ends and depolymerizes F-actin at its pointed end.
“Dephosphorylated cofilin at its serine-3 residue (dp-cofilin) cleaves F-actin to generate new barbed ends that are sites for actin polymerization and depolymerizes F-actin at its pointed end to reduce fiber length.”
From State-dependent diffusion of actin-depolymerizing factor/cofilin underlies the enlargement and shrinkage of dendritic spines (2016) · cites this paper as [15]
Cofilin depolymerizes and cleaves F-actins.
“Cofilin depolymerizes and cleaves F-actins15.”
From State-dependent diffusion of actin-depolymerizing factor/cofilin underlies the enlargement and shrinkage of dendritic spines (2016) · cites this paper as [15]
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Mizuno, K. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2012.11.001 · Cited by 396 · see citing works
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Alhadidi, Q., & Shah, Z. A. (2018) · Molecular Neurobiology · doi:10.1007/s12035-017-0432-7 · Cited by 83 · see citing works
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Aan, G. J., Hairi, H. A., Makpol, S., Rahman, M. A., & Karsani, S. A. (2013) · ELECTROPHORESIS · doi:10.1002/elps.201300086 · Cited by 36 · see citing works
Bao, Z., Han, X., Chen, F., Jia, X., Zhao, J., Zhang, C., Yong, C., Tian, S., Zhou, X., & Han, L. (2015) · BMC Microbiology · doi:10.1186/s12866-015-0500-y · Cited by 26 · see citing works
- Authors
- Van Troys, M., Huyck, L., Leyman, S., Dhaese, S., Vandekerkhove, J., & Ampe, C.
- Affiliations
- Ghent University (BE)
- ORCID
- Huyck, Lynn
- Venue
- European Journal of Cell Biology
- Publisher
- Elsevier BV
- Published
- 2008-09
- Volume
- 87
- Issue
- 8-9
- Pages
- 649-667
- ISSN
- 0171-9335 (ISSN-L)
- OpenAlex
- W1976100793
- Cited by
- 329
- References
- 0
- Citations by year
- 2026: 2 · 2025: 6 · 2024: 9 · 2023: 7 · 2022: 7 · 2021: 11 · 2020: 15 · 2019: 11 · 2018: 17 · 2017: 20 · 2016: 21 · 2015: 22 · 2014: 28 · 2013: 36 · 2012: 39
- FWCI
- 2.06
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- European Journal of Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Ghent University Academic Bibliography (Ghent University) (submittedVersion)
- Funders
- Fonds Wetenschappelijk Onderzoek
- Vlaamse regering
- 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 › Molecular Biology › Mechanisms of cancer metastasis
- Keywords
- ADF/cofilin, actin-binding proteins, actin dynamics, cell migration, tumor invasion, signaling pathways, actin depolymerization, actin polymerization
- MeSH terms
- Actins, Animals, Binding Sites, Cell Movement, Humans, Neoplasms, Phosphorylation, Signal Transduction, Protein Isoforms, Actin Depolymerizing Factors
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