CoChat
Sign Up
Cited by 35Alzheimer's disease research and treatmentsNeuroinflammation and Neurodegeneration MechanismsDementia and Cognitive Impairment Research

Role of Cofilin in Alzheimer’s Disease

Open access
Wang, Qiang, Yuan, Wei, Yang, Xiaohang, Wang, Yuan, Li, Yongfeng, Qiao, Haifa·2020·Frontiers in Cell and Developmental Biology
DOI 10.3389/fcell.2020.584898PMC PMC7726191
Open this paper in CoChat — free accountOpen PDF

Abstract

Alzheimer’s disease (AD) is a degenerative neurological disease and has an inconspicuous onset and progressive development. Clinically, it is characterized by severe dementia manifestations, including memory impairment, aphasia, apraxia, loss of recognition, impairment of visual-spatial skills, executive dysfunction, and changes in personality and behavior. Its etiology is unknown to date. However, several cellular biological signatures of AD have been identified such as synaptic dysfunction, β-amyloid plaques, hyperphosphorylated tau, cofilin-actin rods, and Hirano bodies which are related to the actin cytoskeleton. Cofilin is one of the most affluent and common actin-binding proteins and plays a role in cell motility, migration, shape, and metabolism. They also play an important role in severing actin filament, nucleating, depolymerizing, and bundling activities. In this review, we summarize the structure of cofilins and their functional and regulating roles, focusing on the synaptic dysfunction, β-amyloid plaques, hyperphosphorylated tau, cofilin-actin rods, and Hirano bodies of AD.

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.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.3389/fcell.2020.584898

Cites

14 of 14 references verified0 citation errors · 0 not checkable

Statistics

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.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • CFL1 is one of the main components of actin/cofilin rods, which are insoluble aggregates that lead to neurodysfunction.

    “CFL1 is one of the main components of actin/cofilin rods, which are insoluble aggregates that lead to neurodysfunction [4, 101].”

    From Enhanced microglial dynamics and a paucity of tau seeding in the amyloid plaque microenvironment contribute to cognitive resilience in Alzheimer’s disease (2024) · cites this paper as [101]

    The Introduction identifies CFL1 as the gene encoding cofilin-1, and the Cofilin-Actin Rods section describes rods containing ADF/cofilin and actin in a 1:1 ratio. That section calls them rod-shaped filament bundles, but does not establish that they are insoluble aggregates or that the rods themselves cause neuronal dysfunction; the Conclusion discusses dysfunction involving cofilin more generally. Page numbers are unavailable in our copy. (LLM, conf=0.82)

    Experimental — accuracy not yet measured

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

Flagged first, then by citations

Research works printed but not linked: 174

  1. Agnew B. J. Minamide L. S. Bamburg J. R. (1995). Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site. J. Biol. Chem. 270 17582– 17587. 10.1074/jbc.270.29.17582 7615564 · DOI
  2. Akamatsu M. Vasan R. Serwas D. Ferrin M. A. Rangamani P. Drubin D. G. (2020). Principles of self-organization and load adaptation by the actin cytoskeleton during clathrin-mediated endocytosis. Elife 9: e49840. PMC7041948 31951196
  3. Albiges-Rizo C. Destaing O. Fourcade B. Planus E. Block M. R. (2009). Actin machinery and mechanosensitivity in invadopodia, podosomes and focal adhesions. J. Cell. Sci. 122 3037– 3049. 10.1242/jcs.052704 19692590 PMC2767377 · DOI
  4. Ampe C. Van Troys M. (2017). Mammalian Actins: Isoform-Specific Functions and Diseases. Handb. Exp. Pharmacol. 235 1– 37. 10.1007/164_2016_43 27757757 · DOI
  5. Aragona M. Panciera T. Manfrin A. Giulitti S. Michielin F. Elvassore N. (2013). A mechanical checkpoint controls multicellular growth through YAP/TAZ regulation by actin-processing factors. Cell 154 1047– 1059. 10.1016/j.cell.2013.07.042 23954413 · DOI · Paper page
  6. Augustine R. C. Vidali L. Kleinman K. P. Bezanilla M. (2008). Actin depolymerizing factor is essential for viability in plants, and its phosphoregulation is important for tip growth. Plant J. 54 863– 875. 10.1111/j.1365-313x.2008.03451.x 18298672 · DOI
  7. Bamburg J. R. Bernstein B. W. (2010). Roles of ADF/cofilin in actin polymerization and beyond. F1000 Biol. Rep. 2: 62. PMC2990448 21173851
  8. Bamburg J. R. Bernstein B. W. (2016). Actin dynamics and cofilin-actin rods in alzheimer disease. Cytoskeleton 73 477– 497. 10.1002/cm.21282 26873625 PMC5345344 · DOI · Paper page
  9. Bamburg J. R. Bloom G. S. (2009). Cytoskeletal pathologies of Alzheimer disease. Cell Motil. Cytoskeleton 66 635– 649. 10.1002/cm.20388 19479823 PMC2754410 · DOI
  10. Bamburg J. R. Bloom G. S. (2010). Cytoskeletal pathologies of Alzheimer disease. Cell Motil. Cytoskeleton 66 635– 649. PMC2754410 19479823
  11. Bamburg J. R. Wiggan O. N. P. (2003). N.P., ADF/cofilin and actin dynamics in disease. Trends Cell Biol. 12 598– 605. 10.1016/s0962-8924(02)02404-2 12495849 · DOI
  12. Bannerman D. M. Sprengel R. (2010). Multiple memory mechanisms? The long and the short of it. EMBO J. 29 1790– 1791. 10.1038/emboj.2010.90 20517333 PMC2885926 · DOI
  13. Barone E. Mosser S. Fraering P. C. (2014). Inactivation of brain Cofilin-1 by age, Alzheimer’s disease and γ-secretase. Biochim. Biophys. Acta 1842 2500– 2509. 10.1016/j.bbadis.2014.10.004 25315299 · DOI
  14. Beaty B. T. Condeelis J. (2014). Digging a little deeper: the stages of invadopodium formation and maturation. Eur. J. Cell Biol. 93 438– 444. 10.1016/j.ejcb.2014.07.003 25113547 PMC4262566 · DOI
  15. Beli P. Mascheroni D. Xu D. Innocenti M. (2008). WAVE and Arp2/3 jointly inhibit filopodium formation by entering into a complex with mDia2. Nat. Cell Biol. 10 849– 857. 10.1038/ncb1745 18516090 · DOI
  16. Bellenchi G. C. Gurniak C. B. Perlas E. Middei S. Ammassari-Teule M. Witke W. (2007). N-cofilin is associated with neuronal migration disorders and cell cycle control in the cerebral cortex. Genes Dev. 21 2347– 2357. 10.1101/gad.434307 17875668 PMC1973148 · DOI
  17. Benzing W. C. Brady D. R. Mufson E. J. Armstrong D. M. (1993). Evidence that transmitter-containing dystrophic neurites precede those containing paired helical filaments within senile plaques in the entorhinal cortex of nondemented elderly and Alzheimer’s disease patients. Brain Res. 619 55– 68. 10.1016/0006-8993(93)91595-j 7690677 · DOI
  18. Bernstein B. W. Painter W. B. Chen H. Minamide L. S. Abe H. Bamburg J. R. (2000). Intracellular pH modulation of ADF/cofilin proteins. Cell Motil. Cytoskeleton 47 319– 336. 10.1002/1097-0169(200012)47:4<319::aid-cm6>3.0.co;2-i 11093252 · DOI
  19. Bernstein B. W. Shaw A. E. Minamide L. S. Pak C. W. Bamburg J. R. (2012). Incorporation of cofilin into rods depends on disulfide intermolecular bonds: implications for actin regulation and neurodegenerative disease. J. Neurosci. 32 6670– 6681. 10.1523/jneurosci.6020-11.2012 22573689 PMC3745285 · DOI
  20. Bie B. Wu J. Foss J. F. Naguib M. (2018). Amyloid fibrils induce dysfunction of hippocampal glutamatergic silent synapses. Hippocampus 28 549– 556. 10.1002/hipo.22955 29704282 PMC6133714 · DOI
  21. Blanchoin L. Boujemaa-Paterski R. Sykes C. Plastino J. (2014). Actin dynamics, architecture, and mechanics in cell motility. Physiol. Rev. 94 235– 263. 10.1152/physrev.00018.2013 24382887 · DOI
  22. Blanpied T. A. Ehlers M. D. (2004). Microanatomy of dendritic spines: emerging principles of synaptic pathology in psychiatric and neurological disease. Biol. Psych. 55 1121– 1127. 10.1016/j.biopsych.2003.10.006 15184030 · DOI
  23. Braak H. Braak E. (1995). Staging of Alzheimer’s disease-related neurofibrillary changes. Neurobiol. Aging 16 271– 278. 10.1016/0197-4580(95)00021-6 7566337 · DOI · Paper page
  24. Bravo-Cordero J. J. Magalhaes M. A. Eddy R. J. Hodgson L. Condeelis J. (2013). Functions of cofilin in cell locomotion and invasion. Nat. Rev. Mole. Cell Biol. 14 405– 415. 10.1038/nrm3609 23778968 PMC3878614 · DOI
  25. Buée L. Bussière T. Buée-Scherrer V. Delacourte A. Hof P. R. (2000). Tau protein isoforms, phosphorylation and role in neurodegenerative disorders. Brain Res. Rev. 33 95– 130. 10.1016/s0165-0173(00)00019-9 10967355 · DOI
  26. Chan C. Beltzner C. C. Pollard T. D. (2009). Cofilin dissociates Arp2/3 complex and branches from actin filaments. Curr. Biol. 19 537– 545. 10.1016/j.cub.2009.02.060 19362000 PMC3711486 · DOI
  27. Chang C. Y. Leu J. D. Lee Y. J. (2015). The actin depolymerizing factor (ADF)/cofilin signaling pathway and DNA damage responses in cancer. Int. J. Mol. Sci. 16 4095– 4120. 10.3390/ijms16024095 25689427 PMC4346946 · DOI
  28. Chen L. Y. Rex C. S. Casale M. S. Gall C. M. Lynch G. (2007). Changes in synaptic morphology accompany actin signaling during LTP. J. Neurosci. 27 5363– 5372. 10.1523/jneurosci.0164-07.2007 17507558 PMC6672340 · DOI · Paper page
  29. Chen Q. Courtemanche N. Pollard T. D. (2015). Aip1 promotes actin filament severing by cofilin and regulates constriction of the cytokinetic contractile ring. J. Biol. Chem. 290 2289– 2300. 10.1074/jbc.m114.612978 25451933 PMC4303679 · DOI
  30. Collingridge G. L. Isaac J. T. R. Wang Y.T. (2004). Receptor trafficking and synaptic plasticity. Nat. Rev. Neurosci. 5 952– 962. 15550950
  31. Cummings D. M. Liu W. Erik P. Sevinç B. Marina Y. Sui-Hin H. (2015). First effects of rising amyloid-β in transgenic mouse brain: synaptic transmission and gene expression. Brain 138 1992– 2004. 10.1093/brain/awv127 25981962 PMC4572488 · DOI
  32. Davis R. C. Furukawa R. Fechheimer M. (2008). A cell culture model for investigation of Hirano bodies. Acta Neuropathol. 115 205– 217. 10.1007/s00401-007-0275-9 17978823 · DOI
  33. Davis R. C. Maloney M. T. Minamide L. S. Flynn K. C. Stonebraker M. A. Bamburg J. R. (2009). Mapping cofilin-actin rods in stressed hippocampal slices and the role of cdc42 in amyloid-beta-induced rods. J. Alzheimers Dis. 18 35– 50. 10.3233/jad-2009-1122 19542631 PMC4477627 · DOI
  34. Davis R. C. Marsden I. T. Maloney M. T. Minamide L. S. Podlisny M. Selkoe D. J. (2011). Amyloid beta dimers/trimers potently induce cofilin-actin rods that are inhibited by maintaining cofilin-phosphorylation. Mol. Neurodegener. 6: 10. 10.1186/1750-1326-6-10 21261978 PMC3037337 · DOI
  35. Deshpande A. Mina E. Glabe C. Busciglio J. (2006). Different conformations of amyloid beta induce neurotoxicity by distinct mechanisms in human cortical neurons. J. Neurosci. 26 6011– 6018. 10.1523/jneurosci.1189-06.2006 16738244 PMC6675207 · DOI
  36. dos Remedios C. G. Chhabra D. Kekic M. Dedova I. V. Tsubakihara M. Berry D. A. (2003). Actin binding proteins: regulation of cytoskeletal microfilaments. Physiol. Rev. 83 433– 473. 10.1152/physrev.00026.2002 12663865 · DOI
  37. Dumpich M. Mannherz H. G. Theiss C. (2015). VEGF Signaling Regulates Cofilin and the Arp2/3-complex within the Axonal Growth Cone. Curr. Neurovasc. Res. 12 293– 307. 10.2174/1567202612666150603141144 26036972 · DOI
  38. Edwards D. C. Sanders L. C. Bokoch G. M. Gill G. N. (1999). Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. Nat. Cell Biol. 1 253– 259. 10.1038/12963 10559936 · DOI
  39. Eiseler T. Döppler H. Yan I. K. Kitatani K. Mizuno K. Storz P. (2009). Protein kinase D1 regulates cofilin-mediated F-actin reorganization and cell motility through slingshot. Nat. Cell Biol. 11 545– 556. 10.1038/ncb1861 19329994 PMC2761768 · DOI
  40. Fedulov V. Rex C. S. Simmons D. A. Palmer L. Gall C. M. Lynch G. (2007). Evidence that long-term potentiation occurs within individual hippocampal synapses during learning. J. Neurosci. 27 8031– 8039. 10.1523/jneurosci.2003-07.2007 17652593 PMC6672739 · DOI
  41. Foote M. Qiao H. Graham K. Wu Y. Zhou Y. (2015). Inhibition of 14-3-3 Proteins Leads to Schizophrenia-Related Behavioral Phenotypes and Synaptic Defects in Mice. Biol. Psychiatry 78 386– 395. 10.1016/j.biopsych.2015.02.015 25863357 PMC4544659 · DOI
  42. Foster T. C. Kyritsopoulos C. Kumar A. (2017). Central role for NMDA receptors in redox mediated impairment of synaptic function during aging and Alzheimer’s disease. Behav. Brain Res. 322 223– 232. 10.1016/j.bbr.2016.05.012 27180169 · DOI
  43. Fratelli M. Demol H. Puype M. Casagrande S. Eberini I. Salmona M. (2002). Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes. Proc. Natl. Acad. Sci. U S A. 99 3505– 3510. 10.1073/pnas.052592699 11904414 PMC122553 · DOI
  44. Fukazawa Y. Saitoh Y. Ozawa F. Ohta Y. Mizuno K. Inokuchi K. (2003). is accompanied by enhanced F-actin content within the dendritic spine that is essential for late LTP maintenance in vivo. Neuron 38 447– 460. 10.1016/s0896-6273(03)00206-x 12741991 · DOI · Paper page
  45. Fulga T. A. Elson-Schwab I. Khurana V. Steinhilb M. L. Spires T. L. Hyman B. T. (2007). Abnormal bundling and accumulation of F-actin mediates tau-induced neuronal degeneration in vivo. Nat. Cell Biol. 9 139– 148. 10.1038/ncb1528 17187063 · DOI · Paper page
  46. Galloway P. G. Perry G. Gambetti P. (1987). Hirano Body Filaments Contain Actin and Actin-Associated Proteins. J. Neuropathol. Exper. Neurol. 46 185– 199. 10.1097/00005072-198703000-00006 3029338 · DOI
  47. Gau D. M. Lesnock J. L. Hood B. L. Bhargava R. Sun M. Darcy K. (2015). BRCA1 deficiency in ovarian cancer is associated with alteration in expression of several key regulators of cell motility - A proteomics study. Cell Cycle 14 1884– 1892. 10.1080/15384101.2015.1036203 25927284 PMC4614952 · DOI
  48. Goedert M. (2006). Tau Protein and the Neurofibrillary Pathology of Alzheimer’s Disease. Anna. N Y Acad. Sci. 777 121– 131. 10.1111/j.1749-6632.1996.tb34410.x 8624074 · DOI
  49. Goedert M. (2010). Tau Protein and the Neurofibrillary Pathology of Alzheimer’s Disease. Anna. N Y Acad. Sci. 777 121– 131. 8624074
  50. Gohla A. Bokoch G. M. (2002). 14-3-3 regulates actin dynamics by stabilizing phosphorylated cofilin. Curr. Biol. 12 1704– 1710. 10.1016/s0960-9822(02)01184-3 12361576 · DOI
  51. Goodson M. Rust M. B. Witke W. Bannerman D. Mott R. Ponting C. P. (2012). Cofilin-1: a modulator of anxiety in mice. PLoS Genet. 8: e1002970. 10.1371/journal.pgen.1002970 23055942 PMC3464202 · DOI
  52. Görlich A. Wolf M. Zimmermann A. M. Gurniak C. B. Al Banchaabouchi M. Sassoè-Pognetto M. (2011). N-cofilin can compensate for the loss of ADF in excitatory synapses. PLoS One 6: e26789. 10.1371/journal.pone.0026789 22046357 PMC3203908 · DOI
  53. Gu J. Lee C. W. Fan Y. Komlos D. Tang X. Sun C. (2010). ADF/cofilin-mediated actin dynamics regulate AMPA receptor trafficking during synaptic plasticity. Nat. Neurosci. 13 1208– 1215. 10.1038/nn.2634 20835250 PMC2947576 · DOI
  54. Gu Z. Cheng J. Zhong P. Qin L. Liu W. Yan Z. (2014). Aβ selectively impairs mGluR7 modulation of NMDA signaling in basal forebrain cholinergic neurons: implication in Alzheimer’s disease. J. Neurosci. 34 13614– 13628. 10.1523/jneurosci.1204-14.2014 25297090 PMC6608374 · DOI
  55. Han F. Zhuang T. T. Chen J. J. Zhu X. L. Cai Y. F. Lu Y. P. (2017). Novel derivative of Paeonol, Paeononlsilatie sodium, alleviates behavioral damage and hippocampal dendritic injury in Alzheimer’s disease concurrent with cofilin1/phosphorylated-cofilin1 and RAC1/CDC42 alterations in rats. PLoS One 12: e0185102. 10.1371/journal.pone.0185102 28934273 PMC5608314 · DOI
  56. Hardy J. A. Higgins G. A. (1992). Alzheimer’s disease: the amyloid cascade hypothesis. Science 256 184– 185. 1566067
  57. Heredia L. Helguera P. de Olmos S. Kedikian G. Solá Vigo F. LaFerla F. (2006). Phosphorylation of actin-depolymerizing factor/cofilin by LIM-kinase mediates amyloid beta-induced degeneration: a potential mechanism of neuronal dystrophy in Alzheimer’s disease. J. Neurosci. 26 6533– 6542. 10.1523/jneurosci.5567-05.2006 16775141 PMC6674046 · DOI
  58. Hild G. Kalmár L. Kardos R. Nyitrai M. Bugyi B. (2014). The other side of the coin: Functional and structural versatility of ADF/cofilins. Eur. J. Cell Biol. 93 238– 251. 10.1016/j.ejcb.2013.12.001 24836399 · DOI
  59. Hirano A. (1994). Hirano bodies and related neuronal inclusions. Neuropathol. Appl. Neurobiol. 20 3– 11. 10.1111/j.1365-2990.1994.tb00951.x 8208338 · DOI · Paper page
  60. Holtzman D. M. Mandelkow E. Selkoe D. J. (2012). Alzheimer Disease in 2020. Cold Spring Harbor Perspect. Med. 2 705– 709. PMC3543098 23125202
  61. Homma K. Niino Y. Hotta K. Oka K. (2008). Ca 2+ influx through P2X receptors induces actin cytoskeleton reorganization by the formation of cofilin rods in neurites. Mole. Cell. Neurosci. 37 261– 270. 10.1016/j.mcn.2007.10.001 17993279 · DOI
  62. Honkura N. Matsuzaki M. Noguchi J. Ellis-Davies G. C. Kasai H. (2008). The subspine organization of actin fibers regulates the structure and plasticity of dendritic spines. Neuron 57 719– 729. 10.1016/j.neuron.2008.01.013 18341992 · DOI · Paper page
  63. Hotulainen P. Llano O. Smirnov S. Tanhuanpää K. Faix J. Rivera C. (2009). Defining mechanisms of actin polymerization and depolymerization during dendritic spine morphogenesis. J. Cell Biol. 185 323– 339. 10.1083/jcb.200809046 19380880 PMC2700375 · DOI · Paper page
  64. Huang T. Y. DerMardirossian C. Bokoch G. M. (2006). Cofilin phosphatases and regulation of actin dynamics. Curr. Opin. Cell Biol. 18 26– 31. 10.1016/j.ceb.2005.11.005 16337782 · DOI
  65. Huang T. Y. Minamide L. S. Bamburg J. R. Bokoch G. M. (2008). Chronophin mediates an ATP-sensing mechanism for cofilin dephosphorylation and neuronal cofilin-actin rod formation. Dev. Cell 15 691– 703. 10.1016/j.devcel.2008.09.017 19000834 PMC2644054 · DOI
  66. Ikonomovic M. D. Klunk W. E. Abrahamson E. E. Mathis C. A. Price J. C. Tsopelas N. D. (2008). Post-mortem correlates of in vivo PiB-PET amyloid imaging in a typical case of Alzheimer’s disease. Brain 131 1630– 1645. 10.1093/brain/awn016 18339640 PMC2408940 · DOI · Paper page
  67. Inagaki N. Katsuno H. (2017). Actin Waves: Origin of Cell Polarization and Migration? Trends Cell Biol. 27 515– 526. 10.1016/j.tcb.2017.02.003 28283221 · DOI
  68. Ivanov A. I. McCall I. C. Parkos C. A. Nusrat A. (2004). Role for actin filament turnover and a myosin II motor in cytoskeleton-driven disassembly of the epithelial apical junctional complex. Mol. Biol. Cell 15 2639– 2651. 10.1091/mbc.e04-02-0163 15047870 PMC420089 · DOI
  69. Ivanovska J. Tregubova A. Mahadevan V. Chakilam S. Gandesiri M. Benderska N. (2013). Identification of DAPK as. Int. J. Biochem. Cell Biol. 45 1720– 1729. 23702034
  70. Jack C. R. Jr. Holtzman D. M. (2013). Biomarker modeling of Alzheimer’s disease. Neuron 80 1347– 1358. 24360540 PMC3928967
  71. Jack C. R. Knopman D. S. Jagust W. J. Petersen R. C. Weiner M. W. Aisen P. S. (2013). Tracking pathophysiological processes in Alzheimer’s disease: an updated hypothetical model of dynamic biomarkers. Lancet Neurol. 12 207– 216. 10.1016/s1474-4422(12)70291-0 23332364 PMC3622225 · DOI · Paper page
  72. Jang D. H. Han J. H. Lee S. H. Lee Y. S. Park H. Lee S. H. (2005). Cofilin expression induces cofilin-actin rod formation and disrupts synaptic structure and function in Aplysia synapses. Proc. Natl. Acad. Sci. U S A. 102 16072– 16077. 10.1073/pnas.0507675102 16247020 PMC1276089 · DOI
  73. Jin M. Shepardson N. Yang T. Chen G. Walsh D. Selkoe D. J. (2011). Soluble amyloid beta-protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration. Proc. Natl. Acad. Sci. U S A. 108 5819– 5824. 10.1073/pnas.1017033108 21421841 PMC3078381 · DOI · Paper page
  74. Kanellos G. Frame M. C. (2016). Cellular functions of the ADF/cofilin family at a glance. J. Cell. Sci. 129 3211– 3218. 10.1242/jcs.187849 27505888 · DOI
  75. Kim J. S. Huang T. Y. Bokoch G. M. (2009). Reactive oxygen species regulate a slingshot-cofilin activation pathway. Mol. Biol. Cell 20 2650– 2660. 10.1091/mbc.e09-02-0131 19339277 PMC2688545 · DOI
  76. Kim T. Vidal G. S. Djurisic M. William C. M. Birnbaum M. E. Garcia K. C. (2013). Human LilrB2 is a β-amyloid receptor and its murine homolog PirB regulates synaptic plasticity in an Alzheimer’s model. Science 341 1399– 1404. 10.1126/science.1242077 24052308 PMC3853120 · DOI · Paper page
  77. Klamt F. Zdanov S. Levine R. L. Pariser A. Zhang Y. Zhang B. (2009). Oxidant-induced apoptosis is mediated by oxidation of the actin-regulatory protein cofilin. Nat. Cell Biol. 11 1241– 1246. 10.1038/ncb1968 19734890 PMC3393095 · DOI
  78. Klemke M. Wabnitz G. H. Funke F. Funk B. Kirchgessner H. Samstag Y. (2008). Oxidation of cofilin mediates T cell hyporesponsiveness under oxidative stress conditions. Immunity 29 404– 413. 10.1016/j.immuni.2008.06.016 18771940 · DOI
  79. Konietzny A. Bär J. Mikhaylova M. (2017). Dendritic Actin Cytoskeleton: Structure, Functions, and Regulations. Front. Cell Neurosci. 11: 147. 10.3389/fncel.2017.00147 28572759 PMC5435805 · DOI
  80. Kosaka K. Yoshimura M. Ikeda K. Budka H. (1984). Diffuse type of Lewy body disease: Progressive dementia with abundant cortical Lewy bodies and senile changes of varying degree - A new disease? Clin. Neuropathol. 3 185– 192. 6094067
  81. Kurita S. Watanabe Y. Gunji E. Ohashi K. Mizuno K. (2008). Molecular dissection of the mechanisms of substrate recognition and F-actin-mediated activation of cofilin-phosphatase Slingshot-1. J. Biol. Chem. 283 32542– 32552. 10.1074/jbc.m804627200 18809681 · DOI
  82. Kuznetsov S. A. Rivera D. T. Severin F. F. Weiss D. G. Langford G. M. (2010). Movement of axoplasmic organelles on actin filaments from skeletal muscle. Cytoskeleton 28 231– 242. 10.1002/cm.970280306 7954851 · DOI
  83. Lakshmana M. K. Chung J. Y. Wickramarachchi S. Tak E. Bianchi E. Koo E. H. (2010). A fragment of the scaffolding protein RanBP9 is increased in Alzheimer’s disease brains and strongly potentiates amyloid-beta peptide generation. FASEB J. 24 119– 127. 10.1096/fj.09-136457 19729516 PMC2797034 · DOI
  84. Lakshmana M. K. Yoon I. S. Chen E. Bianchi E. Koo E. H. Kang D. E. (2009). Novel role of RanBP9 in BACE1 processing of amyloid precursor protein and amyloid beta peptide generation. J. Biol. Chem. 284 11863– 11872. 10.1074/jbc.m807345200 19251705 PMC2673255 · DOI
  85. Lappalainen P. Kessels M. M. Cope M. J. Drubin D. G. The A. D. F. (1998). homology (ADF-H) domain: a highly exploited actin-binding module. Mol. Biol. Cell 9 1951– 1959. 10.1091/mbc.9.8.1951 9693358 PMC25446 · DOI
  86. Lee Y. J. Mazzatti D. J. Zhong Y. Keng P. C. (2005). Inhibition of invasiveness of human lung cancer cell line H1299 by over-expression of cofilin. Cell Biol. Int. 29 877– 883. 10.1016/j.cellbi.2005.07.005 16301112 · DOI
  87. Lu L. I. Fu N. I. Luo X. U. Li X. Y. Li X. P. (2015). Overexpression of cofilin 1 in prostate cancer and the corresponding clinical implications. Oncol. Lett. 9 2757– 2761. 10.3892/ol.2015.3133 26137141 PMC4473706 · DOI
  88. Maciver S. K. Harrington C. R. (1995). Two actin binding proteins, actin depolymerizing factor and cofilin, are associated with Hirano bodies. Neuroreport 6 1985– 1988. 10.1097/00001756-199510010-00008 8580423 · DOI
  89. Madsen C. D. Hooper S. Tozluoglu M. Bruckbauer A. Fletcher G. Erler J. T. (2015). STRIPAK components determine mode of cancer cell migration and metastasis. Nat. Cell Biol. 17 68– 80. 10.1038/ncb3083 25531779 PMC5354264 · DOI
  90. Makioka A. Kumagai M. Hiranuka K. Kobayashi S. Takeuchi T. (2011). Entamoeba invadens: identification of ADF/cofilin and their expression analysis in relation to encystation and excystation. Exp. Parasitol. 127 195– 201. 10.1016/j.exppara.2010.07.018 20691182 · DOI
  91. Malenka R. C. Bear M. F. (2004). LTP and LTD: an embarrassment of riches. Neuron 44 5– 21. 15450156
  92. Maloney M. T. Bamburg J. R. (2007). Cofilin-mediated neurodegeneration in Alzheimer’s disease and other amyloidopathies. Mol. Neurobiol. 35 21– 44. 10.1007/s12035-007-0009-y 17519504 · DOI
  93. Maloney M. T. Minamide L. S. Kinley A. W. Boyle J. A. Bamburg J. R. (2005). Beta-secretase-cleaved amyloid precursor protein accumulates at actin inclusions induced in neurons by stress or amyloid beta: a feedforward mechanism for Alzheimer’s disease. J. Neurosci. 25 11313– 11321. 10.1523/jneurosci.3711-05.2005 16339026 PMC6725891 · DOI
  94. Maselli A. G. Davis R. Furukawa R. Fechheimer M. (2002). Formation of Hirano bodies in Dictyostelium and mammalian cells induced by expression of a modified form of an actin-crosslinking protein. J. Cell. Sci. 115 1939– 1949. 11956325
  95. Matus A. Ackermann M. Pehling G. Byers H. R. Fujiwara K. (1982). High actin concentrations in brain dendritic spines and postsynaptic densities. Proc. Natl. Acad. Sci. U S A. 79 7590– 7594. 10.1073/pnas.79.23.7590 6760199 PMC347386 · DOI · Paper page
  96. Mendoza-Naranjo A. Contreras-Vallejos E. Henriquez D. R. Otth C. Bamburg J. R. Maccioni R. B. (2012). Fibrillar amyloid-β1-42 modifies actin organization affecting the cofilin phosphorylation state: a role for Rac1/cdc42 effector proteins and the slingshot phosphatase. J. Alzheimers Dis. 29 63– 77. 10.3233/jad-2012-101575 22204905 · DOI
  97. Mikati M. A. Breitsprecher D. Jansen S. Reisler E. Goode B. L. (2015). Coronin Enhances Actin Filament Severing by Recruiting Cofilin to Filament Sides and Altering F-Actin Conformation. J. Mol. Biol. 427 3137– 3147. 10.1016/j.jmb.2015.08.011 26299936 PMC4579047 · DOI
  98. Minamide L. S. Maiti S. Boyle J. A. Davis R. C. Coppinger J. A. Bao Y. (2010). Isolation and characterization of cytoplasmic cofilin-actin rods. J. Biol. Chem. 285 5450– 5460. 10.1074/jbc.m109.063768 20022956 PMC2820773 · DOI
  99. Minamide L. S. Striegl A. M. Boyle J. A. Meberg P. J. Bamburg J. R. (2000). Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function. Nat. Cell Biol. 2 628– 636. 10.1038/35023579 10980704 · DOI
  100. Morgan T. E. Lockerbie R. O. Minamide L. S. Browning M. D. Bamburg J. R. (1993). Isolation and characterization of a regulated form of actin depolymerizing factor. J. Cell Biol. 122 623– 633. 10.1083/jcb.122.3.623 7687605 PMC2119666 · DOI
  101. Moriyama K. Iida K. Yahara I. (1996). Phosphorylation of Ser-3 of cofilin regulates its essential function on actin. Genes Cells 1 73– 86. 10.1046/j.1365-2443.1996.05005.x 9078368 · DOI
  102. Mullins R. D. Hansen S. D. (2013). In vitro studies of actin filament and network dynamics. Curr. Opin. Cell Biol. 25 6– 13. 10.1016/j.ceb.2012.11.007 23267766 PMC3578108 · DOI
  103. Nader K. Krysiak A. Beroun A. Pekala M. Szymanska M. Kuzniewska B. (2019). Loss of serum response factor in mature neurons in the dentate gyrus alters the morphology of dendritic spines and hippocampus-dependent behavioral tasks. Brain Struct. Funct. 224 2691– 2701. 10.1007/s00429-019-01925-6 31375980 PMC6778544 · DOI
  104. Nagata-Ohashi K. Ohta Y. Goto K. Chiba S. Mori R. Nishita M. (2004). A pathway of neuregulin-induced activation of cofilin-phosphatase Slingshot and cofilin in lamellipodia. J. Cell Biol. 165 465– 471. 10.1083/jcb.200401136 15159416 PMC2172350 · DOI
  105. Nimchinsky E. A. Sabatini B. L. Svoboda K. (2002). Structure and function of dendritic spines. Ann. Rev. Physiol. 64 313– 353. 11826272
  106. Niwa R. Nagata-Ohashi K. Takeichi M. Mizuno K. Uemura T. (2002). Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin. Cell 108 233– 246. 10.1016/s0092-8674(01)00638-9 11832213 · DOI
  107. Nomura K. Hayakawa K. Tatsumi H. Ono S. (2016). Actin-interacting Protein 1 Promotes Disassembly of Actin-depolymerizing Factor/Cofilin-bound Actin Filaments in a pH-dependent Manner. J. Biol. Chem. 291 5146– 5156. 10.1074/jbc.m115.713495 26747606 PMC4777849 · DOI
  108. Ono S. Minami N. Abe H. Obinata T. (1994). Characterization of a novel cofilin isoform that is predominantly expressed in mammalian skeletal muscle. J. Biol. Chem. 269 15280– 15286. 8195165
  109. Paavilainen V. O. Oksanen E. Goldman A. Lappalainen P. (2008). Structure of the actin-depolymerizing factor homology domain in complex with actin. J. Cell Biol. 182 51– 59. 10.1083/jcb.200803100 18625842 PMC2447895 · DOI
  110. Perche O. Laumonnier F. Baala L. Ardourel M. Y. Menuet A. Robin V. (2010). Autism, genetics and synaptic function alterations. Pathol. Biol. 58 381– 386. 20181440
  111. Peterburs P. Heering J. Link G. Pfizenmaier K. Olayioye M. A. Hausser A. (2009). Protein kinase D regulates cell migration by direct phosphorylation of the cofilin phosphatase slingshot 1 like. Cancer Res. 69 5634– 5638. 10.1158/0008-5472.can-09-0718 19567672 · DOI
  112. Peterson C. Kress Y. Vallee R. Goldman J. E. (1988). High molecular weight microtubule-associated proteins bind to actin lattices (Hirano bodies). Acta Neuropathol. 77 168– 174. 3227813
  113. Pollard T. D. Borisy G. G. (2003). Cellular motility driven by assembly and disassembly of actin filaments. Cell 112 453– 465. 10.1016/s0092-8674(03)00120-x 12600310 · DOI
  114. Pontrello C. G. M-Sun Y. Lin A. Fiacco T. A. DeFea K. A. Ethell I. M. (2012). Cofilin under control of p-arrestin-2 in NMDA- dependent dendritic spine plasticity, long-term depression (LTD), and learning. Proc. Natl. Acad. Sci. U S A. 109: 2208. PMC3289389 22308427
  115. Porat-Shliom N. Milberg O. Masedunskas A. Weigert R. (2013). Multiple roles for the actin cytoskeleton during regulated exocytosis. Cell. Mol. Life Sci. 70 2099– 2121. 10.1007/s00018-012-1156-5 22986507 PMC4052552 · DOI · Paper page
  116. Qiao H. Foote M. Graham K. Wu Y. Zhou Y. (2014). 14-3-3 proteins are required for hippocampal long-term potentiation and associative learning and memory. J. Neurosci. 34 4801– 4808. 10.1523/jneurosci.4393-13.2014 24695700 PMC3972712 · DOI
  117. Racz B. Weinberg R. J. (2006). Spatial organization of cofilin in dendritic spines. Neuroscience 138 447– 456. 10.1016/j.neuroscience.2005.11.025 16388910 · DOI
  118. Rahman T. Davies D. S. Tannenberg R. K. Fok S. Shepherd C. Dodd P. R. (2014). Cofilin rods and aggregates concur with tau pathology and the development of Alzheimer’s disease. J. Alzheimers Dis. 42 1443– 1460. 10.3233/jad-140393 25024349 · DOI · Paper page
  119. Rapoport M. Dawson H. N. Binder L. I. Vitek M. P. Ferreira A. (2002). Tau is essential to beta -amyloid-induced neurotoxicity. Proc. Natl. Acad. Sci. U S A. 99 6364– 6369. 11959919 PMC122954
  120. Richmond J. (2005). Synaptic function. Wormbook Online Rev. C Elegans Biol. 30 1– 14. PMC4781477 18050398
  121. Roberson E. D. Scearce-Levie K. Palop J. J. Yan F. Cheng I. H. Wu T. (2007). Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer’s disease mouse model. Science 316 750– 754. 10.1126/science.1141736 17478722 · DOI · Paper page
  122. Rust M. B. Gurniak C. B. Renner M. Vara H. Morando L. Görlich A. (2010). Learning, AMPA receptor mobility and synaptic plasticity depend on n-cofilin-mediated actin dynamics. EMBO J. 29 1889– 1902. 10.1038/emboj.2010.72 20407421 PMC2885936 · DOI
  123. Schmidt M. L. Lee V. M. Trojanowski J. Q. (1989). Analysis of epitopes shared by Hirano bodies and neurofilament proteins in normal and Alzheimer’s disease hippocampus. Lab. Invest. 60 513– 522. 2468822
  124. Schochet S. S. McCormick W. F. (1972). Ultrastructure of Hirano bodies. Acta Neuropathol. 21 50– 60. 10.1007/bf00687999 4340098 · DOI
  125. Senju Y. Lappalainen P. (2019). Regulation of actin dynamics by PI(4,5)P2 in cell migration and endocytosis. Curr. Opin. Cell Biol. 56 7– 13. 10.1016/j.ceb.2018.08.003 30193157 · DOI · Paper page
  126. Shi Y. Pontrello C. G. Defea K. A. Reichardt L. F. Ethell I. M. (2009). Focal Adhesion Kinase Acts Downstream of EphB Receptors to Maintain Mature Dendritic Spines by Regulating Cofilin Activity. J. Neurosci. 29 8129– 8142. 10.1523/jneurosci.4681-08.2009 19553453 PMC2819391 · DOI
  127. Shipton O. A. Leitz J. R. Dworzak J. Acton C. E. Tunbridge E. M. Denk F. (2011). Tau protein is required for amyloid {beta}-induced impairment of hippocampal long-term potentiation. J. Neurosci. 31 1688– 1692. 10.1523/jneurosci.2610-10.2011 21289177 PMC3836238 · DOI · Paper page
  128. Shishkin S. Eremina L. Pashintseva N. Kovalev L. Kovaleva M. (2016). Cofilin-1 and Other ADF/Cofilin Superfamily Members in Human Malignant Cells. Int. J. Mole. Sci. 18: 10. 10.3390/ijms18010010 28025492 PMC5297645 · DOI
  129. Smith-Dijak A. I. Sepers M. D. Raymond L. A. (2019). Alterations in synaptic function and plasticity in Huntington disease. J. Neurochem. 150 346– 365. 10.1111/jnc.14723 31095731 · DOI
  130. Soosairajah J. Maiti S. Wiggan O. Sarmiere P. Moussi N. Sarcevic B. (2005). Interplay between components of a novel LIM kinase-slingshot phosphatase complex regulates cofilin. EMBO J. 24 473– 486. 10.1038/sj.emboj.7600543 15660133 PMC548651 · DOI
  131. Soukup S. F. Vanhauwaert R. Verstreken P. (2018). Parkinson’s disease: convergence on synaptic homeostasis. EMBO J. 37: e98960. PMC6138432 30065071
  132. Sparrow N. Manetti M. E. Bott M. Fabianac T. Petrilli A. Bates M. L. (2012). The actin-severing protein cofilin is downstream of neuregulin signaling and is essential for Schwann cell myelination. J. Neurosci. 32 5284– 5297. 10.1523/jneurosci.6207-11.2012 22496574 PMC3490500 · DOI
  133. Star E. N. Kwiatkowski D. J. Murthy V. N. (2002). Rapid turnover of actin in dendritic spines and its regulation by activity. Nat. Neurosci. 5 239– 246. 10.1038/nn811 11850630 · DOI
  134. Sudhof T. C. (2004). The synaptic vesicle cycle. Annu. Rev. Neurosci. 27 509– 547. 15217342
  135. Südhof T. C. (2013). Neurotransmitter release: the last millisecond in the life of a synaptic vesicle. Neuron 80 675– 690. 10.1016/j.neuron.2013.10.022 24183019 PMC3866025 · DOI · Paper page
  136. Tahtamouni L. H. Shaw A. E. Hasan M. H. Yasin S. R. Bamburg J. R. (2013). Non-overlapping activities of ADF and cofilin-1 during the migration of metastatic breast tumor cells. BMC Cell Biol. 14: 45. 10.1186/1471-2121-14-45 24093776 PMC3850953 · DOI
  137. Tania N. Condeelis J. Edelstein-Keshet L. (2013). Modeling the synergy of cofilin and Arp2/3 in lamellipodial protrusive activity. Biophys. J. 105 1946– 1955. 10.1016/j.bpj.2013.09.013 24209839 PMC3824550 · DOI
  138. Teitelbaum S. L. Zou W. (2011). The Osteoclast Cytoskeleton: How Does It Work? Ibms Bonekey 8 74– 83. 10.1138/20110493 · DOI
  139. Thompson P. M. Hayashi K. M. Dutton R. A. Chiang M. C. Leow A. D. Sowell E. R. (2007). Tracking Alzheimer’s disease. Ann. N Y Acad. Sci. 1097 183– 214. 17413023 PMC3197831
  140. Tomasella A. Blangy A. Brancolini C. (2014). A receptor-interacting protein 1 (RIP1)-independent necrotic death under the control of protein phosphatase PP2A that involves the reorganization of actin cytoskeleton and the action of cofilin-1. J. Biol. Chem. 289 25699– 25710. 10.1074/jbc.m114.575134 25096578 PMC4162173 · DOI
  141. Tomonaga M. (1974). Ultrastructure of Hirano bodies. Acta Neuropathol. 28 365– 366. 10.1007/bf00685292 4446940 · DOI
  142. Toshima J. Toshima J. Y. Takeuchi K. Mori R. Mizuno K. (2001). Cofilin phosphorylation and actin reorganization activities of testicular protein kinase 2 and its predominant expression in testicular Sertoli cells. J. Biol. Chem. 276 31449– 31458. 10.1074/jbc.m102988200 11418599 · DOI
  143. Tsai C. H. Lin L. T. Wang C. Y. Chiu Y. W. Chou Y. T. Chiu S. J. (2015). Over-expression of cofilin-1 suppressed growth and invasion of cancer cells is associated with up-regulation of let-7 microRNA. Biochim. Biophys. Acta 1852 851– 861. 10.1016/j.bbadis.2015.01.007 25597880 · DOI
  144. Tsai J. Grutzendler J. Duff K. Gan W. B. (2004). Fibrillar amyloid deposition leads to local synaptic abnormalities and breakage of neuronal branches. Nat. Neurosci. 7 1181– 1183. 10.1038/nn1335 15475950 · DOI · Paper page
  145. Ueno A. Dautu G. Saiki E. Haga K. Igarashi M. (2010). Toxoplasma gondii deoxyribose phosphate aldolase-like protein (TgDPA) interacts with actin depolymerizing factor (TgADF) to enhance the actin filament dynamics in the bradyzoite stage. Mol. Biochem. Parasitol. 173 39– 42. 10.1016/j.molbiopara.2010.04.007 20433874 · DOI
  146. Vartiainen M. K. Mustonen T. Mattila P. K. Ojala P. J. Thesleff I. Partanen J. (2002). The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin dynamics. Mol. Biol. Cell 13 183– 194. 10.1091/mbc.01-07-0331 11809832 PMC65081 · DOI
  147. Verdile G. Fuller S. Atwood C. S. Laws S. M. Gandy S. E. Martins R. N. (2004). The role of beta amyloid in Alzheimer’s disease: still a cause of everything or the only one who got caught? Pharmacol. Res. 50 397– 409. 10.1016/j.phrs.2003.12.028 15304237 · DOI
  148. Wang W. Eddy R. Condeelis J. (2007). The cofilin pathway in breast cancer invasion and metastasis. Nat. Rev. Cancer 7 429– 440. 10.1038/nrc2148 17522712 PMC4270061 · DOI
  149. Wang W. Mouneimne G. Sidani M. Wyckoff J. Chen X. Makris A. (2006). The activity status of cofilin is directly related to invasion, intravasation, and metastasis of mammary tumors. J. Exper. Med. 173 395– 404. 10.1083/jcb.200510115 16651380 PMC2063840 · DOI
  150. Wang Y. Dong Q. Xu X. F. Feng X. Xin J. Wang D. D. (2013). Phosphorylation of cofilin regulates extinction of conditioned aversive memory via AMPAR trafficking. J. Neurosci. 33 6423– 6433. 10.1523/jneurosci.5107-12.2013 23575840 PMC6619091 · DOI
  151. Wang Y. Shibasaki F. Mizuno K. (2005). Calcium signal-induced cofilin dephosphorylation is mediated by Slingshot via calcineurin. J. Biol. Chem. 280 12683– 12689. 10.1074/jbc.m411494200 15671020 · DOI
  152. Weaver A. M. (2008). Cortactin in tumor invasiveness. Cancer Lett. 265 157– 166. 10.1016/j.canlet.2008.02.066 18406052 PMC2460566 · DOI
  153. Welch M. D. Iwamatsu A. Mitchison T. J. (1997). Actin polymerization is induced by Arp 2/3 protein complex at the surface of Listeria monocytogenes. Nature 385 265– 269. 10.1038/385265a0 9000076 · DOI
  154. Whiteman I. T. Gervasio O. L. Cullen K. M. Guillemin G. J. Jeong E. V. Witting P. K. (2009). Activated actin-depolymerizing factor/cofilin sequesters phosphorylated microtubule-associated protein during the assembly of alzheimer-like neuritic cytoskeletal striations. J. Neurosci. 29 12994– 13005. 10.1523/jneurosci.3531-09.2009 19828813 PMC2821881 · DOI · Paper page
  155. Winder S. J. Ayscough K. R. (2005). Actin-binding proteins. J. Cell. Sci. 118 651– 654. 15701920
  156. Wolf M. Zimmermann A. M. Görlich A. Gurniak C. B. Sassoè-Pognetto M. Friauf E. (2015). ADF/Cofilin Controls Synaptic Actin Dynamics and Regulates Synaptic Vesicle Mobilization and Exocytosis. Cereb. Cortex 25 2863– 2875. 10.1093/cercor/bhu081 24770705 · DOI
  157. Woo J. A. Boggess T. Uhlar C. Wang X. Khan H. Cappos G. (2015a). RanBP9 at the intersection between cofilin and Aβ pathologies: rescue of neurodegenerative changes by RanBP9 reduction. Cell Death Dis. 6: 1676. PMC4385917 25741591
  158. Woo J. A. Jung A. R. Lakshmana M. K. Bedrossian A. Lim Y. Bu J. H. (2012). Pivotal role of the RanBP9-cofilin pathway in Aβ-induced apoptosis and neurodegeneration. Cell Death Differ. 19 1413– 1423. 10.1038/cdd.2012.14 22361682 PMC3422466 · DOI · Paper page
  159. Woo J. A. Liu T. Fang C. C. Cazzaro S. Kee T. LePochat P. (2019). Activated cofilin exacerbates tau pathology by impairing tau-mediated microtubule dynamics. Commun. Biol. 2: 112. PMC6430779 30911686
  160. Woo J. A. Zhao X. Khan H. Penn C. Wang X. Joly-Amado A. (2015b). Slingshot-Cofilin activation mediates mitochondrial and synaptic dysfunction via Aβ ligation to β1-integrin conformers. Cell Death Differ. 22 921– 934. 10.1038/cdd.2015.5 25698445 PMC4423195 · DOI · Paper page
  161. Wu H. Y. Hudry E. Hashimoto T. Kuchibhotla K. Hyman B. T. (2010). Amyloid Induces the Morphological Neurodegenerative Triad of Spine Loss. Dendritic Simplification, and Neuritic Dystrophies through Calcineurin Activation. J. Neurosci. 30 2636– 2649. 10.1523/jneurosci.4456-09.2010 20164348 PMC2841957 · DOI · Paper page
  162. Yamaguchi H. Condeelis J. (2007). Regulation of the actin cytoskeleton in cancer cell migration and invasion. Biochim. Biophys. Acta 1773 642– 652. 10.1016/j.bbamcr.2006.07.001 16926057 PMC4266238 · DOI
  163. Yamashiro S. Mohri K. Ono S. (2005). The two Caenorhabditis elegans actin-depolymerizing factor/cofilin proteins differently enhance actin filament severing and depolymerization. Biochemistry 44 14238– 14247. 10.1021/bi050933d 16245940 PMC1910702 · DOI
  164. Yang N. Higuchi O. Ohashi K. Nagata K. Wada A. Kangawa K. (1998). Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization. Nature 393 809– 812. 10.1038/31735 9655398 · DOI
  165. Yang X. Cao Z. Zhang J. Shao B. Song M. Han Y. (2018). Dendritic spine loss caused by AlCl3 is associated with inhibition of the Rac 1/cofilin signaling pathway. Environ. Pollut. 243 1689– 1695. 10.1016/j.envpol.2018.09.145 30300874 · DOI
  166. Yonezawa N. Homma Y. Yahara I. Sakai H. Nishida E. (1991). A short sequence responsible for both phosphoinositide binding and actin binding activities of cofilin. J. Biol. Chem. 266 17218– 17221. 1654325
  167. Yonezawa N. Nishida E. Sakai H. (1985). pH control of actin polymerization by cofilin. J. Biol. Chem. 260 14410– 14412. 4055781
  168. Yoo Y. Ho H. J. Wang C. Guan J.-L. (2010). Tyrosine phosphorylation of cofilin at Y68 by v-Src leads to its degradation through ubiquitin–proteasome pathway. Oncogene 29 263– 272. 10.1038/onc.2009.319 19802004 PMC2806939 · DOI
  169. Zalli D. Neff L. Nagano K. Shin N. Y. Witke W. Gori F. (2016). The Actin-Binding Protein Cofilin and Its Interaction With Cortactin Are Required for Podosome Patterning in Osteoclasts and Bone Resorption In Vivo and In Vitro. J. Bone Miner. Res. 31 1701– 1712. 10.1002/jbmr.2851 27064822 PMC5070801 · DOI
  170. Zhang H. H. Wang W. Feng L. Yang Y. Zheng J. Huang L. (2015). S-nitrosylation of Cofilin-1 Serves as a Novel Pathway for VEGF-Stimulated Endothelial Cell Migration. J. Cell. Physiol. 230 406– 417. 10.1002/jcp.24724 25056928 PMC8906234 · DOI
  171. Zhao H. Hakala M. Lappalainen P. (2010). ADF/cofilin binds phosphoinositides in a multivalent manner to act as a PIP(2)-density sensor. Biophys. J. 98 2327– 2336. 10.1016/j.bpj.2010.01.046 20483342 PMC2872272 · DOI
  172. Zhou G. L. Zhang H. Field J. Mammalian C. A. P. (2014). (Cyclase-associated protein) in the world of cell migration: Roles in actin filament dynamics and beyond. Cell Adh. Migr. 8 55– 59. 10.4161/cam.27479 24429384 PMC3974795 · DOI
  173. Zimmermann A. M. Jene T. Wolf M. Görlich A. Gurniak C. B. Sassoè-Pognetto M. (2015). Attention-Deficit/Hyperactivity Disorder-like Phenotype in a Mouse Model with Impaired Actin Dynamics. Biol. Psychiatry 78 95– 106. 10.1016/j.biopsych.2014.03.011 24768258 · DOI
  174. Zucker R. S. Regehr W. G. (2002). Short-term synaptic plasticity. Annu. Rev. Physiol. 64 355– 405. 11826273

Cited by

Sorted by citations

Authors
Wang, Q., Yuan, W., Yang, X., Wang, Y., Li, Y., & Qiao, H.
Affiliations
Shaanxi University of Chinese Medicine (CN)
Corresponding author
Qiao, Haifa
ORCID
Venue
Frontiers in Cell and Developmental Biology
Publisher
Frontiers Media SA
Published
2020-11-26
Volume
8
Pages
584898-584898
ISSN
2296-634X (ISSN-L)
DOI
10.3389/fcell.2020.584898
PMC
PMC7726191
OpenAlex
W3110518257
Cited by
35
References
14
Citations by year
2026: 5 · 2025: 2 · 2024: 7 · 2023: 12 · 2022: 6 · 2021: 3
FWCI
0.67
Type
journal article
Language
en
Open access
Licence
Locations
  • Frontiers in Cell and Developmental Biology (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • National Natural Science Foundation of China (81873385)
  • Shaanxi University of Chinese Medicine (YL-09)
Topics
  • Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
  • Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
  • Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords
cofilin, Alzheimer's disease, actin cytoskeleton, actin-binding proteins, synaptic dysfunction, amyloid plaques, hyperphosphorylated tau, Hirano bodies, actin filament dynamics, dementia

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