{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,6]],"date-time":"2026-06-06T04:02:13Z","timestamp":1780718533384,"version":"3.54.1"},"reference-count":40,"publisher":"Pharmaceutical Society of Japan","issue":"6","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biological &amp; Pharmaceutical Bulletin","Biol. Pharm. Bull."],"published-print":{"date-parts":[[2026,6,3]]},"DOI":"10.1248\/bpb.b26-00012","type":"journal-article","created":{"date-parts":[[2026,6,2]],"date-time":"2026-06-02T22:10:01Z","timestamp":1780438201000},"page":"910-918","source":"Crossref","is-referenced-by-count":0,"title":["Ca&lt;sup&gt;2+&lt;\/sup&gt; Regulates Cofilin Nuclear Translocation through Distinct Mechanisms in Rat Basophilic Leukemia Cells"],"prefix":"10.1248","volume":"49","author":[{"given":"Ayaka","family":"Yamamoto","sequence":"first","affiliation":[{"name":"Graduate School of Pharmaceutical Sciences, Nagoya City University, 3\u20131 Tanabe-dori, Mizuho-ku, Nagoya 467\u20138603, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ruriko","family":"Suzuki","sequence":"additional","affiliation":[{"name":"School of Pharmacy, Aichi Gakuin University, 1\u2013100 Kusumoto-cho, Chikusa-ku, Nagoya 464\u20138650, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Masahiko","family":"Tanaka","sequence":"additional","affiliation":[{"name":"Graduate School of Pharmaceutical Sciences, Nagoya City University, 3\u20131 Tanabe-dori, Mizuho-ku, Nagoya 467\u20138603, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tadahide","family":"Furuno","sequence":"additional","affiliation":[{"name":"School of Pharmacy, Aichi Gakuin University, 1\u2013100 Kusumoto-cho, Chikusa-ku, Nagoya 464\u20138650, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Naohide","family":"Hirashima","sequence":"additional","affiliation":[{"name":"Graduate School of Pharmaceutical Sciences, Nagoya City University, 3\u20131 Tanabe-dori, Mizuho-ku, Nagoya 467\u20138603, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"163","reference":[{"key":"1","doi-asserted-by":"crossref","unstructured":"1) Ju Z, Thomas TN, Chiu YJ, Yamanouchi S, Yoshida Y, Abe JI, Takahashi A, Wang J, Fujiwara K, Hada M. Adaptation and changes in actin dynamics and cell motility as early responses of cultured mammalian cells to altered gravitational vector. <i>Int. J. Mol. Sci.<\/i>, <b>23<\/b>, 6127 (2022).","DOI":"10.3390\/ijms23116127"},{"key":"2","doi-asserted-by":"crossref","unstructured":"2) Schaks M, Giannone G, Rottner K. Actin dynamics in cell migration. <i>Essays Biochem.<\/i>, <b>63<\/b>, 483\u2013495 (2019).","DOI":"10.1042\/EBC20190015"},{"key":"3","doi-asserted-by":"crossref","unstructured":"3) Venkatesh K, Mathew A, Koushika SP. Role of actin in organelle trafficking in neurons. <i>Cytoskeleton<\/i>, <b>77<\/b>, 97\u2013109 (2020).","DOI":"10.1002\/cm.21580"},{"key":"4","doi-asserted-by":"crossref","unstructured":"4) Moriyama K, Iida K, Yahara I. Phosphorylation of Ser-3 of cofilin regulates its essential function on actin. <i>Genes Cells<\/i>, <b>1<\/b>, 73\u201386 (1996).","DOI":"10.1046\/j.1365-2443.1996.05005.x"},{"key":"5","doi-asserted-by":"crossref","unstructured":"5) Yang N, Higuchi O, Ohashi K, Nagata K, Wada A, Kangawa K, Nishida E, Mizuno K. Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization. <i>Nature<\/i>, <b>393<\/b>, 809\u2013812 (1998).","DOI":"10.1038\/31735"},{"key":"6","doi-asserted-by":"crossref","unstructured":"6) Mizuno K. Signaling mechanisms and functional roles of cofilin phosphorylation and dephosphorylation. <i>Cell. Signal.<\/i>, <b>25<\/b>, 457\u2013469 (2013).","DOI":"10.1016\/j.cellsig.2012.11.001"},{"key":"7","doi-asserted-by":"crossref","unstructured":"7) Klejnot M, Gabrielsen M, Cameron J, Mleczak A, Talapatra SK, Kozielski F, Pannifer A, Olson MF. Analysis of the human cofilin 1 structure reveals conformational changes required for actin binding. <i>Acta Crystallogr. D Biol. Crystallogr.<\/i>, <b>69<\/b>, 1780\u20131788 (2013).","DOI":"10.1107\/S0907444913014418"},{"key":"8","doi-asserted-by":"crossref","unstructured":"8) Wada A, Fukuda M, Mishima M, Nishida E. Nuclear export of actin: a novel mechanism regulating the subcellular localization of a major cytoskeletal protein. <i>EMBO J.<\/i>, <b>17<\/b>, 1635\u20131641 (1998).","DOI":"10.1093\/emboj\/17.6.1635"},{"key":"9","doi-asserted-by":"crossref","unstructured":"9) Kelpsch DJ, Tootle TL. Nuclear actin: from discovery to function. <i>Anat. Rec.<\/i>, <b>301<\/b>, 1999\u20132013 (2018).","DOI":"10.1002\/ar.23959"},{"key":"10","doi-asserted-by":"crossref","unstructured":"10) Dopie J, Skarp KP, Rajakyl\u00e4 EK, Tanhuanp\u00e4\u00e4 K, Vartiainen MK. Active maintenance of nuclear actin by importin 9 supports transcription. <i>Proc. Natl. Acad. Sci. U.S.A.<\/i>, <b>109<\/b>, E544\u2013E552 (2012).","DOI":"10.1073\/pnas.1118880109"},{"key":"11","doi-asserted-by":"crossref","unstructured":"11) Esteban V, Skrabski F, Perales-Chorda C, Puente-Crespo Y, Mu\u00f1oz-Cano R, Cardona V. Perspectives in the molecular mechanisms underlying anaphylaxis. <i>J. Investig. Allergol. Clin. Immunol.<\/i>, <b>35<\/b>, 251\u2013266 (2025).","DOI":"10.18176\/jiaci.1080"},{"key":"12","doi-asserted-by":"crossref","unstructured":"12) Suzuki R, Inoh Y, Yokawa S, Furuno T, Hirashima N. Monomer hapten and hapten-specific IgG inhibit mast cell activation evoked by multivalent hapten with different mechanisms. <i>Eur. J. Immunol.<\/i>, <b>49<\/b>, 2172\u20132183 (2019).","DOI":"10.1002\/eji.201847973"},{"key":"13","doi-asserted-by":"crossref","unstructured":"13) Scharenberg AM, Lin S, Cuenod B, Yamamura H, Kinet JP. Reconstitution of interactions between tyrosine kinases and the high affinity IgE receptor which are controlled by receptor clustering. <i>EMBO J.<\/i>, <b>14<\/b>, 3385\u20133394 (1995).","DOI":"10.1002\/j.1460-2075.1995.tb07344.x"},{"key":"14","doi-asserted-by":"crossref","unstructured":"14) Suzuki R, Inoh Y, Yokawa S, Furuno T, Hirashima N. Receptor dynamics regulates actin polymerization state through phosphorylation of cofilin in mast cells. <i>Biochem. Biophys. Res. Commun.<\/i>, <b>534<\/b>, 714\u2013719 (2021).","DOI":"10.1016\/j.bbrc.2020.11.012"},{"key":"15","doi-asserted-by":"crossref","unstructured":"15) Maus M, Medgyesi D, Kiss E, Schneider AE, Enyedi A, Szil\u00e1gyi N, Matk\u00f3 J, S\u00e1rmay G. B cell receptor-induced Ca<sup>2+<\/sup> mobilization mediates F-actin rearrangements and is indispensable for adhesion and spreading of B lymphocytes. <i>J. Leukoc. Biol.<\/i>, <b>93<\/b>, 537\u2013547 (2013).","DOI":"10.1189\/jlb.0312169"},{"key":"16","doi-asserted-by":"crossref","unstructured":"16) Freeman SA, Lei V, Dang-Lawson M, Mizuno K, Roskelley CD, Gold MR. Cofilin-mediated F-actin severing is regulated by the Rap GTPase and controls the cytoskeletal dynamics that drive lymphocyte spreading and BCR microcluster formation. <i>J. Immunol.<\/i>, <b>187<\/b>, 5887\u20135900 (2011).","DOI":"10.4049\/jimmunol.1102233"},{"key":"17","doi-asserted-by":"crossref","unstructured":"17) Wabnitz GH, Kirchgessner H, Jahraus B, Umansky L, Shenolikar S, Samstag Y. Protein phosphatase 1\u03b1 and cofilin regulate nuclear translocation of NF-\u03baB and promote expression of the anti-inflammatory cytokine interleukin-10 by T cells. <i>Mol. Cell. Biol.<\/i>, <b>38<\/b>, e00041\u201318 (2018).","DOI":"10.1128\/MCB.00041-18"},{"key":"18","doi-asserted-by":"crossref","unstructured":"18) Samstag Y, Eckerskorn C, Wesselborg S, Henning S, Wallich R, Meuer SC. Costimulatory signals for human T-cell activation induce nuclear translocation of pp19\/cofilin. <i>Proc. Natl. Acad. Sci. U.S.A.<\/i>, <b>91<\/b>, 4494\u20134498 (1994).","DOI":"10.1073\/pnas.91.10.4494"},{"key":"19","doi-asserted-by":"crossref","unstructured":"19) Teshima R, Suzuki K, Ikebuchi H, Terao T. Possible involvement of phosphorylation of a 36,000-dalton protein of rat basophilic leukemia (RBL-2H3) cell membranes in serotonin release. <i>Mol. Immunol.<\/i>, <b>23<\/b>, 279\u2013284 (1986).","DOI":"10.1016\/0161-5890(86)90054-4"},{"key":"20","doi-asserted-by":"crossref","unstructured":"20) Inoh Y, Ito N, Yokawa S, Suzuki R, Furuno T. Surface charge, but not size, of liposomes is involved in the suppression of rat basophilic leukemia (RBL-2H3) cell degranulation mediated by Akt phosphorylation. <i>Cell Biol. Int.<\/i>, <b>48<\/b>, 1463\u20131472 (2024).","DOI":"10.1002\/cbin.12205"},{"key":"21","doi-asserted-by":"crossref","unstructured":"21) Ang WX, Church AM, Kulis M, Choi HW, Burks AW, Abraham SN. Mast cell desensitization inhibits calcium flux and aberrantly remodels actin. <i>J. Clin. Invest.<\/i>, <b>126<\/b>, 4103\u20134118 (2016).","DOI":"10.1172\/JCI87492"},{"key":"22","doi-asserted-by":"crossref","unstructured":"22) Iida K, Matsumoto S, Yahara I. The KKRKK sequence is involved in heat shock-induced nuclear translocation of the 18-kDa actin-binding protein, cofilin. <i>Cell Struct. Funct.<\/i>, <b>17<\/b>, 39\u201346 (1992).","DOI":"10.1247\/csf.17.39"},{"key":"23","doi-asserted-by":"crossref","unstructured":"23) Nishida E, Iida K, Yonezawa N, Koyasu S, Yahara I, Sakai H. Cofilin is a component of intranuclear and cytoplasmic actin rods induced in cultured cells. <i>Proc. Natl. Acad. Sci. U.S.A.<\/i>, <b>84<\/b>, 5262\u20135266 (1987).","DOI":"10.1073\/pnas.84.15.5262"},{"key":"24","doi-asserted-by":"crossref","unstructured":"24) Nebl G, Meuer SC, Samstag Y. Dephosphorylation of serine 3 regulates nuclear translocation of cofilin. <i>J. Biol. Chem.<\/i>, <b>271<\/b>, 26276\u201326280 (1996).","DOI":"10.1074\/jbc.271.42.26276"},{"key":"25","doi-asserted-by":"crossref","unstructured":"25) Xing J, Wang Y, Peng A, Li J, Niu X, Zhang K. The role of actin cytoskeleton CFL1 and ADF\/cofilin superfamily in inflammatory response. <i>Front. Mol. Biosci.<\/i>, <b>11<\/b>, 1408287 (2024).","DOI":"10.3389\/fmolb.2024.1408287"},{"key":"26","doi-asserted-by":"crossref","unstructured":"26) Colin-York H, Li D, Korobchevskaya K, Chang VT, Betzig E, Eggeling C, Fritzsche M. Cytoskeletal actin patterns shape mast cell activation. <i>Commun. Biol.<\/i>, <b>2<\/b>, 93 (2019).","DOI":"10.1038\/s42003-019-0322-9"},{"key":"27","doi-asserted-by":"crossref","unstructured":"27) F\u00f6ger N, Jenckel A, Orinska Z, Lee KH, Chan AC, Bulfone-Paus S. Differential regulation of mast cell degranulation <i>versus<\/i> cytokine secretion by the actin regulatory proteins Coronin1a and Coronin1b. <i>J. Exp. Med.<\/i>, <b>208<\/b>, 1777\u20131787 (2011).","DOI":"10.1084\/jem.20101757"},{"key":"28","doi-asserted-by":"crossref","unstructured":"28) Filho EGF, da Silva EZM, Ong HL, Swaim WD, Ambudkar IS, Oliver C, Jamur MC. RACK1 plays a critical role in mast cell secretion and Ca<sup>2+<\/sup> mobilization by modulating F-actin dynamics. <i>J. Cell Sci.<\/i>, <b>134<\/b>, jcs252585 (2021).","DOI":"10.1242\/jcs.252585"},{"key":"29","doi-asserted-by":"crossref","unstructured":"29) Deng Z, Zink T, Chen HY, Walters D, Liu FT, Liu GY. Impact of actin rearrangement and degranulation on the membrane structure of primary mast cells: a combined atomic force and laser scanning confocal microscopy investigation. <i>Biophys. J.<\/i>, <b>96<\/b>, 1629\u20131639 (2009).","DOI":"10.1016\/j.bpj.2008.11.015"},{"key":"30","doi-asserted-by":"crossref","unstructured":"30) Obrdlik A, Percipalle P. The F-actin severing protein cofilin-1 is required for RNA polymerase II transcription elongation. <i>Nucleus<\/i>, <b>2<\/b>, 72\u201379 (2011).","DOI":"10.4161\/nucl.2.1.14508"},{"key":"31","doi-asserted-by":"crossref","unstructured":"31) Ohta Y, Nishida E, Sakai H, Miyamoto E. Dephosphorylation of cofilin accompanies heat shock-induced nuclear accumulation of cofilin. <i>J. Biol. Chem.<\/i>, <b>264<\/b>, 16143\u201316148 (1989).","DOI":"10.1016\/S0021-9258(18)71598-6"},{"key":"32","doi-asserted-by":"crossref","unstructured":"32) Munsie L, Caron N, Atwal RS, Marsden I, Wild EJ, Bamburg JR, Tabrizi SJ, Truant R. Mutant huntingtin causes defective actin remodeling during stress: defining a new role for transglutaminase 2 in neurodegenerative disease. <i>Hum. Mol. Genet.<\/i>, <b>20<\/b>, 1937\u20131951 (2011).","DOI":"10.1093\/hmg\/ddr075"},{"key":"33","doi-asserted-by":"crossref","unstructured":"33) Pendleton A, Pope B, Weeds A, Koffer A. Latrunculin B or ATP depletion induces cofilin-dependent translocation of actin into nuclei of mast cells. <i>J. Biol. Chem.<\/i>, <b>278<\/b>, 14394\u201314400 (2003).","DOI":"10.1074\/jbc.M206393200"},{"key":"34","doi-asserted-by":"crossref","unstructured":"34) Nosworthy NJ, Kekic M, dos Remedios CG. The affinity of chick cofilin for actin increases when actin is complexed with DNase I: formation of a cofilin-actin-DNase I ternary complex. <i>Proteomics<\/i>, <b>1<\/b>, 1513\u20131518 (2001).","DOI":"10.1002\/1615-9861(200111)1:12<1513::AID-PROT1513>3.0.CO;2-K"},{"key":"35","doi-asserted-by":"crossref","unstructured":"35) Eulitz D, Mannherz HG. Inhibition of deoxyribonuclease I by actin is to protect cells from premature cell death. <i>Apoptosis<\/i>, <b>12<\/b>, 1511\u20131521 (2007).","DOI":"10.1007\/s10495-007-0078-4"},{"key":"36","doi-asserted-by":"crossref","unstructured":"36) Liu G, Han S, Jiang S, Jiang Y, Chen C, Na Sun, Che H. Extracellular Ca2+ aggravates IgE-induced allergic reaction in mast cells through GPRC6A, a novel family C G-protein-coupled receptor. <i>Life Sci<\/i>, <b>311<\/b>(Pt. A), 121013 (2022).","DOI":"10.1016\/j.lfs.2022.121013"},{"key":"37","doi-asserted-by":"crossref","unstructured":"37) Zhao JW, Gao ZL, Zhang HY, Ji QY, Wang H, Yang YD, Xing FJ, Meng LJ, Wang Y. Regulation of cofilin activity by CaMKII and calcineurin. <i>Am. J. Med. Sci.<\/i>, <b>344<\/b>, 462\u2013472 (2012).","DOI":"10.1097\/MAJ.0b013e318244745b"},{"key":"38","doi-asserted-by":"crossref","unstructured":"38) Takemura M, Mishima T, Wang Y, Kasahara J, Fukunaga K, Ohashi K, Mizuno K. Ca<sup>2+<\/sup>\/calmodulin-dependent protein kinase IV-mediated LIM kinase activation is critical for calcium signal-induced neurite outgrowth. <i>J. Biol. Chem.<\/i>, <b>284<\/b>, 28554\u201328562 (2009).","DOI":"10.1074\/jbc.M109.006296"},{"key":"39","doi-asserted-by":"crossref","unstructured":"39) Toshima J, Toshima JY, Amano T, Yang N, Narumiya S, Mizuno K. Cofilin phosphorylation by protein kinase testicular protein kinase 1 and its role in integrin-mediated actin reorganization and focal adhesion formation. <i>Mol. Biol. Cell<\/i>, <b>12<\/b>, 1131\u20131145 (2001).","DOI":"10.1091\/mbc.12.4.1131"},{"key":"40","doi-asserted-by":"crossref","unstructured":"40) Sakuma M, Shirai Y, Yoshino K, Kuramasu M, Nakamura T, Yanagita T, Mizuno K, Hide I, Nakata Y, Saito N. Novel PKC\u03b1-mediated phosphorylation site(s) on cofilin and their potential role in terminating histamine release. <i>Mol. Biol. Cell<\/i>, <b>23<\/b>, 3707\u20133721 (2012).","DOI":"10.1091\/mbc.e12-01-0053"}],"container-title":["Biological and Pharmaceutical Bulletin"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.jstage.jst.go.jp\/article\/bpb\/49\/6\/49_b26-00012\/_pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,6,6]],"date-time":"2026-06-06T03:32:48Z","timestamp":1780716768000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.jstage.jst.go.jp\/article\/bpb\/49\/6\/49_b26-00012\/_article"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,6,3]]},"references-count":40,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2026]]}},"URL":"https:\/\/doi.org\/10.1248\/bpb.b26-00012","relation":{},"ISSN":["0918-6158","1347-5215"],"issn-type":[{"value":"0918-6158","type":"print"},{"value":"1347-5215","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,6,3]]},"article-number":"b26-00012"}}