Signaling mechanisms and functional roles of cofilin phosphorylation and dephosphorylation
Abstract
Cofilin and actin-depolymerizing factor (ADF) are actin-binding proteins that play an essential role in regulating actin filament dynamics and reorganization by stimulating the severance and depolymerization of actin filaments. Cofilin/ADF are inactivated by phosphorylation at the serine residue at position 3 by LIM-kinases (LIMKs) and testicular protein kinases (TESKs) and are reactivated by dephosphorylation by the slingshot (SSH) family of protein phosphatases and chronophin. This review describes recent advances in our understanding of the signaling mechanisms regulating LIMKs and SSHs and the functional roles of cofilin phospho-regulation in cell migration, tumor invasion, mitosis, neuronal development, and synaptic plasticity. Accumulating evidence demonstrates that the phospho-regulation of cofilin/ADF is a key convergence point of cell signaling networks that link extracellular stimuli to actin cytoskeletal dynamics and that spatiotemporal control of cofilin/ADF activity by LIMKs and SSHs plays a crucial role in a diverse array of cellular and physiological processes. Perturbations in the normal control of cofilin/ADF activity underlie many pathological conditions, including cancer metastasis and neurological and cardiovascular disorders.
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Reelin signaling activates PI3kinase, which initiates a pathway that induces phosphorylation of LIM kinase-1 (LIMK-1), which in turn phosphorylates cofilin at an inhibitory site, blocking the actin-depolymerizing activity of cofilin.
“Reelin signaling activates PI3kinase, as described above [61]. In turn, PI3kinase initiates a signaling pathway that induces phosphorylation of LIM kinase-1 (LIMK-1), which in turn phosphorylates cofilin at an inhibitory site, blocking the actin-depolymerizing activity of cofilin [62, 63].”
From ApoE, ApoE Receptors, and the Synapse in Alzheimer's Disease (2017) · cites this paper as [63]
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p57Kip2 Regulates Actin Dynamics by Binding and Translocating LIM-kinase 1 to the Nucleus
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Impaired Spermatogenic Ability of Testicular Germ Cells in Mice Deficient in the LIM-Kinase 2 Gene
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LIMK1 and CLIP‐115: linking cytoskeletal defects to Williams syndrome
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Self-citationDirect stimulation of receptor‐controlled phospholipase D1 by phospho‐cofilin
Han, L., Stope, M. B., de Jesús, M. L., Weernink, P. A. O., Urban, M., Wieland, T., Rosskopf, D., Mizuno, K., Jakobs, K. H., & Schmidt, M. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601852 · Cited by 99 · see citing works
Self-citationKiz-1, a protein with LIM zinc finger and kinase domains, is expressed mainly in neurons.
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Kiuchi, T., Nagai, T., Ohashi, K., & Mizuno, K. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201101035 · Cited by 95 · see citing works
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LIMK-1 and LIMK-2, two members of a LIM motif-containing protein kinase family.
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Nischarin Inhibits LIM Kinase To Regulate Cofilin Phosphorylation and Cell Invasion
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ALDH1L1 inhibits cell motility via dephosphorylation of cofilin by PP1 and PP2A
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The phosphorylation of p25/TPPP by LIM kinase 1 inhibits its ability to assemble microtubules
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Self-citationCaspase‐mediated cleavage and activation of LIM‐kinase 1 and its role in apoptotic membrane blebbing
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Concentration of cofilin, a small actin‐binding protein, at the cleavage furrow during cytokinesis
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Protein Kinase D Regulates Cofilin Activity through p21-activated Kinase 4
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Self-citationThe N-terminal LIM domain negatively regulates the kinase activity ofLIM-kinase 1
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Self-citationKurita, S., Watanabe, Y., Gunji, E., Ohashi, K., & Mizuno, K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804627200 · Cited by 56 · see citing works
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Actopaxin Interacts with TESK1 to Regulate Cell Spreading on Fibronectin
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Cytoplasmic Localization of LIM-Kinase 1 Is Directed by a Short Sequence within the PDZ Domain
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Self-citationMitosis-Dependent Phosphorylation and Activation of LIM-Kinase 1
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Coronin 2A regulates a subset of focal-adhesion-turnover events through the cofilin pathway
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Self-citationEphA Signaling Promotes Actin-based Dendritic Spine Remodeling through Slingshot Phosphatase
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Actin filaments‐stabilizing and ‐bundling activities of cofilin‐phosphatase Slingshot‐1
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Identification of multiple actin‐binding sites in cofilin‐phosphatase Slingshot‐1L
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LIM-kinase is critical for the mesenchymal-to-amoeboid cell morphological transition in 3D matrices
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Self-citation14-3-3ζ/τ heterodimers regulate Slingshot activity in migrating keratinocytes
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Phosphorylation of Ser 402 impedes phosphatase activity of slingshot 1
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Crystal structure of human slingshot phosphatase 2
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Slingshot‐3 dephosphorylates ADF/cofilin but is dispensable for mouse development
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Phagocytosis: Receptors, signal integration, and the cytoskeleton
Freeman, S. A., & Grinstein, S. (2014) · Immunological Reviews · doi:10.1111/imr.12212 · Cited by 548 · see citing works
ApoE, ApoE Receptors, and the Synapse in Alzheimer's Disease
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“In turn, PI3kinase initiates a signaling pathway that induces phosphorylation of LIM kinase-1 (LIMK-1), which in turn phosphorylates cofilin at an inhibitory site, blocking the actindepolymerizing activity of cofilin [62, 63].”
BackgroundPyronneau, A., He, Q., Hwang, J.-Y., Porch, M., Contractor, A., & Zukin, R. S. (2017) · Science Signaling · doi:10.1126/scisignal.aan0852 · Cited by 122 · see citing works
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Maldonado-Contreras, A., Birtley, J. R., Boll, E., Zhao, Y., Mumy, K. L., Toscano, J., Ayehunie, S., Reinecker, H.-C., Stern, L. J., & McCormick, B. A. (2017) · Gut Microbes · doi:10.1080/19490976.2017.1339006 · Cited by 57 · see citing works
Xu, X., Gera, N., Li, H., Yun, M., Zhang, L., Wang, Y., Wang, Q. J., & Jin, T. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-05-0982 · Cited by 55 · see citing works
Zhang, C., Chen, F., Liu, X., Han, X., Hu, Y., Su, X., Chen, Y., Sun, Y., & Han, L. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.01345 · Cited by 29 · 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
Complex Roles of Annexin A2 in Host Blood–Brain Barrier Invasion by <i>Cryptococcus neoformans</i>
Fang, W., Fa, Z., Xie, Q., Wang, G., Yi, J., Zhang, C., Meng, G., Gu, J., & Liao, W. (2017) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.12673 · Cited by 24 · see citing works
- Authors
- Mizuno, K.
- Affiliations
- Tohoku University (JP)
- Corresponding author
- Mizuno, Kensaku
- ORCID
- Mizuno, Kensaku
- Venue
- Cellular Signalling
- Publisher
- Elsevier BV
- Published
- 2013-02
- Volume
- 25
- Issue
- 2
- Pages
- 457-469
- ISSN
- 0898-6568 (ISSN-L)
- OpenAlex
- W2030777833
- Cited by
- 396
- References
- 154
- Citations by year
- 2026: 18 · 2025: 23 · 2024: 22 · 2023: 25 · 2022: 19 · 2021: 38 · 2020: 27 · 2019: 24 · 2018: 39 · 2017: 41 · 2016: 29 · 2015: 35 · 2014: 33 · 2013: 21 · 2012: 1
- FWCI
- 2.64
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Cellular Signalling (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Ministry of Education, Culture, Sports, Science and Technology
- 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 › Neuroscience › Cellular and Molecular Neuroscience › Axon Guidance and Neuronal Signaling
- Keywords
- cofilin, actin depolymerizing factor, cofilin phosphorylation, cofilin dephosphorylation, LIM kinase, actin cytoskeleton dynamics, cell migration, tumor invasion, mitosis, neuronal development, synaptic plasticity, metastasis, cardiovascular disease, neurological disorders
- MeSH terms
- Actins, Animals, Humans, Neoplasms, Phosphoprotein Phosphatases, Phosphorylation, Signal Transduction, Protein Serine-Threonine Kinases, 14-3-3 Proteins, Actin Depolymerizing Factors
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.
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