{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,10]],"date-time":"2026-09-10T05:07:53Z","timestamp":1789016873265,"version":"build-2803163510"},"reference-count":51,"publisher":"MDPI AG","issue":"17","license":[{"start":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T00:00:00Z","timestamp":1788393600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000024","name":"CIHR","doi-asserted-by":"publisher","award":["MOP-142250"],"award-info":[{"award-number":["MOP-142250"]}],"id":[{"id":"10.13039\/501100000024","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000024","name":"CIHR","doi-asserted-by":"publisher","award":["519474"],"award-info":[{"award-number":["519474"]}],"id":[{"id":"10.13039\/501100000024","id-type":"DOI","asserted-by":"publisher"}]},{"award":["MOP-142250"],"award-info":[{"award-number":["MOP-142250"]}],"id":[{"id":"https:\/\/ror.org\/01gavpb45","id-type":"ROR","asserted-by":"publisher"}]},{"award":["519474"],"award-info":[{"award-number":["519474"]}],"id":[{"id":"https:\/\/ror.org\/01gavpb45","id-type":"ROR","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001804","name":"Canada Research Chair","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100001804","id-type":"DOI","asserted-by":"crossref"}]},{"name":"Natural Sciences Research Council","award":["RGPIN-2024-04314"],"award-info":[{"award-number":["RGPIN-2024-04314"]}]},{"DOI":"10.13039\/501100000196","name":"Canada Foundation for Innovation","doi-asserted-by":"crossref","award":["#225404"],"award-info":[{"award-number":["#225404"]}],"id":[{"id":"10.13039\/501100000196","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100000196","name":"Canada Foundation for Innovation","doi-asserted-by":"crossref","award":["#30865"],"award-info":[{"award-number":["#30865"]}],"id":[{"id":"10.13039\/501100000196","id-type":"DOI","asserted-by":"crossref"}]},{"award":["#225404"],"award-info":[{"award-number":["#225404"]}],"id":[{"id":"https:\/\/ror.org\/000az4664","id-type":"ROR","asserted-by":"publisher"}]},{"award":["#30865"],"award-info":[{"award-number":["#30865"]}],"id":[{"id":"https:\/\/ror.org\/000az4664","id-type":"ROR","asserted-by":"publisher"}]},{"name":"Ontario Research Fund","award":["RE010-020"],"award-info":[{"award-number":["RE010-020"]}]},{"name":"Ontario Research Fund","award":["#34876"],"award-info":[{"award-number":["#34876"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cells"],"abstract":"<jats:p>Adseverin is a Ca2+-dependent, actin severing protein that promotes fusion of osteoclast precursors in osteoclast formation. Currently it is not understood how actin severing activity is regulated in osteoclastogenesis. Mass spectrometry of adseverin immunoprecipitates from osteoclasts showed that adseverin associated with Serpin D1. Purified Serpin D1 interacted with adseverin in vitro in a Ca2+-dependent manner. Ca2+ increased actin severing by ~2-fold. Cells that differentiated into osteoclasts expressed an intracellular, truncated Serpind1 isoform that lacked exons 1 and 2, and part of exon 3. This truncated Serpin D1 isoform was distinct from the secreted, full-length Serpin D1 protein that inhibits thrombin activity. The expression of truncated Serpin D1 in RAW264.7 cells appeared to be further increased following TNF-\u03b1 treatment during RANKL-induced osteoclastogenesis. CRISPR\/Cas9-mediated partial deletion of exon 3 of Serpind1, which resulted in Serpind1 knockout, increased the abundance of subcortical actin filaments. This treatment also altered the spatial distribution of adseverin, inhibited the expression of osteoclast-specific genes and reduced the formation of multinucleated osteoclasts by &gt;90% in vitro. We conclude that a truncated, intracellular variant of Serpin D1 interacts with adseverin to promote actin severing and osteoclast formation.<\/jats:p>","DOI":"10.3390\/cells15171607","type":"journal-article","created":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T16:21:21Z","timestamp":1788452481000},"page":"1607","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["A Truncated Serpin D1 Variant Regulates Adseverin-Dependent Actin Severing and Is Required for Osteoclastogenesis"],"prefix":"10.3390","volume":"15","author":[{"ORCID":"https:\/\/orcid.org\/0009-0002-2629-8979","authenticated-orcid":false,"given":"Yongqiang","family":"Wang","sequence":"first","affiliation":[{"name":"Faculty of Dentistry, University of Toronto, Toronto, ON M5G 1G6, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chenfan","family":"Ji","sequence":"additional","affiliation":[{"name":"Faculty of Dentistry, University of Toronto, Toronto, ON M5G 1G6, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9123-8214","authenticated-orcid":false,"given":"Andrew Y.","family":"Wang","sequence":"additional","affiliation":[{"name":"Faculty of Dentistry, University of Toronto, Toronto, ON M5G 1G6, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Masoud","family":"Norouzi","sequence":"additional","affiliation":[{"name":"Faculty of Dentistry, University of Toronto, Toronto, ON M5G 1G6, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Isabel","family":"Ding","sequence":"additional","affiliation":[{"name":"Faculty of Dentistry, University of Toronto, Toronto, ON M5G 1G6, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6248-5977","authenticated-orcid":false,"given":"Michael","family":"Glogauer","sequence":"additional","affiliation":[{"name":"Faculty of Dentistry, University of Toronto, Toronto, ON M5G 1G6, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mark","family":"Abovsky","sequence":"additional","affiliation":[{"name":"Osteoarthritis Research Program, Division of Orthopedic Surgery, Schroeder Arthritis Institute and Data Science Discovery Centre for Chronic Diseases, Krembil Research Institute, University Health Network, Toronto, ON M5T 0S8, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Igor","family":"Jurisica","sequence":"additional","affiliation":[{"name":"Faculty of Dentistry, University of Toronto, Toronto, ON M5G 1G6, Canada"},{"name":"Osteoarthritis Research Program, Division of Orthopedic Surgery, Schroeder Arthritis Institute and Data Science Discovery Centre for Chronic Diseases, Krembil Research Institute, University Health Network, Toronto, ON M5T 0S8, Canada"},{"name":"Departments of Medical Biophysics and Computer Science, University of Toronto, Toronto, ON M5G 1L7, Canada"},{"name":"Institute of Neuroimmunology, Slovak Academy of Sciences, 845 10 Bratislava, Slovakia"},{"name":"Biological and Life Sciences Division, School of Digital Public Health, Mohamed bin Zayed University of Artificial Intelligence, Masdar City, Abu Dhabi 200120, United Arab Emirates"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3535-8593","authenticated-orcid":false,"given":"Christopher A.","family":"McCulloch","sequence":"additional","affiliation":[{"name":"Faculty of Dentistry, University of Toronto, Toronto, ON M5G 1G6, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,9,3]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"14932","DOI":"10.1021\/acsami.5b08126","article-title":"Study of Osteoclast Adhesion to Cortical Bone Surfaces: A Correlative Microscopy Approach for Concomitant Imaging of Cellular Dynamics and Surface Modifications","volume":"8","author":"Shemesh","year":"2016","journal-title":"ACS Appl. Mater. Interfaces"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"434","DOI":"10.4049\/jimmunol.163.1.434","article-title":"Osteoclast differentiation factor acts as a multifunctional regulator in murine osteoclast differentiation and function","volume":"163","author":"Jimi","year":"1999","journal-title":"J. Immunol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1993","DOI":"10.1182\/bloodadvances.2017008540","article-title":"Macrophages and osteoclasts stem from a bipotent progenitor downstream of a macrophage\/osteoclast\/dendritic cell progenitor","volume":"1","author":"Xiao","year":"2017","journal-title":"Blood Adv."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1097\/00003086-197610000-00030","article-title":"The osteoclast: Review of ultrastructure, origin, and structure-function relationship","volume":"120","author":"Gothlin","year":"1976","journal-title":"Clin. Orthop. Relat. Res."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1111\/j.1365-2613.2000.00164.x","article-title":"Osteoclasts and giant cells: Macrophage-macrophage fusion mechanism","volume":"81","author":"Vignery","year":"2000","journal-title":"Int. J. Exp. Pathol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"3597","DOI":"10.1073\/pnas.95.7.3597","article-title":"Osteoclast differentiation factor is a ligand for osteoprotegerin\/osteoclastogenesis-inhibitory factor and is identical to TRANCE\/RANKL","volume":"95","author":"Yasuda","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/S0092-8674(00)81569-X","article-title":"Osteoprotegerin ligand is a cytokine that regulates osteoclast differentiation and activation","volume":"93","author":"Lacey","year":"1998","journal-title":"Cell"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"526","DOI":"10.1016\/0006-291X(91)92015-C","article-title":"Macrophage colony stimulating factor (M-CSF) is essential for osteoclast formation in vitro","volume":"177","author":"Hattersley","year":"1991","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1007\/s00223-014-9864-5","article-title":"Osteoclast fusion is based on heterogeneity between fusion partners","volume":"95","author":"Delaisse","year":"2014","journal-title":"Calcif. Tissue Int."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"1715","DOI":"10.1016\/j.bbamcr.2015.04.001","article-title":"Role of actin filaments in fusopod formation and osteoclastogenesis","volume":"1853","author":"Wang","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1007\/978-1-4020-6191-2_21","article-title":"Calcium signalling and calcium transport in bone disease","volume":"45","author":"Blair","year":"2007","journal-title":"Subcell. Biochem."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"758","DOI":"10.1038\/nature02444","article-title":"Costimulatory signals mediated by the ITAM motif cooperate with RANKL for bone homeostasis","volume":"428","author":"Koga","year":"2004","journal-title":"Nature"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"35209","DOI":"10.1074\/jbc.M505815200","article-title":"Nuclear factor of activated T cells c1 induces osteoclast-associated receptor gene expression during tumor necrosis factor-related activation-induced cytokine-mediated osteoclastogenesis","volume":"280","author":"Kim","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"4776","DOI":"10.4238\/2014.July.2.7","article-title":"New roles of filopodia and podosomes in the differentiation and fusion process of osteoclasts","volume":"13","author":"Song","year":"2014","journal-title":"Genet. Mol. Res."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"3120","DOI":"10.1091\/mbc.e11-01-0086","article-title":"Podosome rings generate forces that drive saltatory osteoclast migration","volume":"22","author":"Hu","year":"2011","journal-title":"Mol. Biol. Cell"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1016\/j.bbrc.2007.11.106","article-title":"Functional grouping of osteoclast genes revealed through microarray analysis","volume":"366","author":"Yang","year":"2008","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Hassanpour, S., Jiang, H., Wang, Y., Kuiper, J.W., and Glogauer, M. (2014). The actin binding protein adseverin regulates osteoclastogenesis. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0109078"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1007\/s00223-017-0271-6","article-title":"Deletion of Adseverin in Osteoclasts Affects Cell Structure But Not Bone Metabolism","volume":"101","author":"Cao","year":"2017","journal-title":"Calcif. Tissue Int."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"2281","DOI":"10.1096\/fj.14-265744","article-title":"Adseverin plays a role in osteoclast differentiation and periodontal disease-mediated bone loss","volume":"29","author":"Jiang","year":"2015","journal-title":"FASEB J."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1084\/jem.191.2.275","article-title":"Tumor necrosis factor alpha stimulates osteoclast differentiation by a mechanism independent of the ODF\/RANKL-RANK interaction","volume":"191","author":"Kobayashi","year":"2000","journal-title":"J. Exp. Med."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"100282","DOI":"10.1016\/j.bonr.2020.100282","article-title":"Osteoclasts and their circulating precursors in rheumatoid arthritis: Relationships with disease activity and bone erosions","volume":"12","author":"Carrier","year":"2020","journal-title":"Bone Rep."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1016\/j.tibs.2006.06.005","article-title":"Shape-shifting serpins--advantages of a mobile mechanism","volume":"31","author":"Huntington","year":"2006","journal-title":"Trends Biochem. Sci."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1055\/s-0031-1276582","article-title":"Heparin cofactor II: Discovery, properties, and role in controlling vascular homeostasis","volume":"37","author":"Rau","year":"2011","journal-title":"Semin. Thromb. Hemost."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"3775","DOI":"10.1172\/JCI35711","article-title":"NFATc1 in mice represses osteoprotegerin during osteoclastogenesis and dissociates systemic osteopenia from inflammation in cherubism","volume":"118","author":"Aliprantis","year":"2008","journal-title":"J. Clin. Investig."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"902","DOI":"10.1016\/j.bone.2012.08.113","article-title":"The collection of NFATc1-dependent transcripts in the osteoclast includes numerous genes non-essential to physiologic bone resorption","volume":"51","author":"Charles","year":"2012","journal-title":"Bone"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1172\/JCI0213432","article-title":"Heparin cofactor II inhibits arterial thrombosis after endothelial injury","volume":"109","author":"He","year":"2002","journal-title":"J. Clin. Investig."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1514","DOI":"10.1172\/JCI27095","article-title":"Strain-dependent embryonic lethality and exaggerated vascular remodeling in heparin cofactor II-deficient mice","volume":"117","author":"Aihara","year":"2007","journal-title":"J. Clin. Investig."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"3077","DOI":"10.1111\/jcmm.14277","article-title":"Overview of RAW264.7 for osteoclastogensis study: Phenotype and stimuli","volume":"23","author":"Kong","year":"2019","journal-title":"J. Cell Mol. Med."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"jcs213967","DOI":"10.1242\/jcs.213967","article-title":"IL1beta and TNFalpha promote RANKL-dependent adseverin expression and osteoclastogenesis","volume":"131","author":"Wang","year":"2018","journal-title":"J. Cell Sci."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"734","DOI":"10.1091\/mbc.e12-10-0754","article-title":"Collagen remodeling by phagocytosis is determined by collagen substrate topology and calcium-dependent interactions of gelsolin with nonmuscle myosin IIA in cell adhesions","volume":"24","author":"Arora","year":"2013","journal-title":"Mol. Biol. Cell"},{"key":"ref_31","doi-asserted-by":"crossref","unstructured":"Chicaybam, L., Barcelos, C., Peixoto, B., Carneiro, M., Limia, C.G., Redondo, P., Lira, C., Paraguassu-Braga, F., Vasconcelos, Z.F., and Barros, L. (2016). An Efficient Electroporation Protocol for the Genetic Modification of Mammalian Cells. Front. Bioeng. Biotechnol., 4.","DOI":"10.3389\/fbioe.2016.00099"},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Liu, H., and Naismith, J.H. (2008). An efficient one-step site-directed deletion, insertion, single and multiple-site plasmid mutagenesis protocol. BMC Biotechnol., 8.","DOI":"10.1186\/1472-6750-8-91"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"4589","DOI":"10.1128\/MCB.18.8.4589","article-title":"Murine adseverin (D5), a novel member of the gelsolin family, and murine adseverin are induced by interleukin-9 in T-helper lymphocytes","volume":"18","author":"Robbens","year":"1998","journal-title":"Mol. Cell Biol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1481","DOI":"10.1172\/JCI11176","article-title":"TNF-alpha induces osteoclastogenesis by direct stimulation of macrophages exposed to permissive levels of RANK ligand","volume":"106","author":"Lam","year":"2000","journal-title":"J. Clin. Investig."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"466","DOI":"10.1016\/j.ejcb.2014.06.003","article-title":"Dock-family exchange factors in cell migration and disease","volume":"93","author":"Gadea","year":"2014","journal-title":"Eur. J. Cell Biol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/j.bone.2017.08.006","article-title":"Spontaneous mutation of Dock7 results in lower trabecular bone mass and impaired periosteal expansion in aged female Misty mice","volume":"105","author":"Le","year":"2017","journal-title":"Bone"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"e199","DOI":"10.1038\/emm.2015.94","article-title":"Adseverin mediates RANKL-induced osteoclastogenesis by regulating NFATc1","volume":"47","author":"Song","year":"2015","journal-title":"Exp. Mol. Med."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1359\/JBMR.0301238","article-title":"Actin-related protein 2\/3 complex is required for actin ring formation","volume":"19","author":"Hurst","year":"2004","journal-title":"J. Bone Miner. Res."},{"key":"ref_39","doi-asserted-by":"crossref","unstructured":"Han, G., Zuo, J., and Holliday, L.S. (2019). Specialized Roles for Actin in Osteoclasts: Unanswered Questions and Therapeutic Opportunities. Biomolecules, 9.","DOI":"10.3390\/biom9010017"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"2291","DOI":"10.1016\/j.yexcr.2010.05.011","article-title":"Morphological and proteomic analysis of early stage of osteoblast differentiation in osteoblastic progenitor cells","volume":"316","author":"Hong","year":"2010","journal-title":"Exp. Cell Res."},{"key":"ref_41","doi-asserted-by":"crossref","unstructured":"Blangy, A., Touaitahuata, H., Cres, G., and Pawlak, G. (2012). Cofilin activation during podosome belt formation in osteoclasts. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0045909"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1701","DOI":"10.1002\/jbmr.2851","article-title":"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","volume":"31","author":"Zalli","year":"2016","journal-title":"J. Bone Miner. Res."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"979","DOI":"10.1016\/j.bbamcr.2010.11.002","article-title":"Calcium signaling in osteoclasts","volume":"1813","author":"Hwang","year":"2011","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1186\/1479-7364-7-22","article-title":"Update of the human and mouse SERPIN gene superfamily","volume":"7","author":"Heit","year":"2013","journal-title":"Hum. Genom."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1002\/j.1460-2075.1990.tb08078.x","article-title":"Chromaffin cell scinderin, a novel calcium-dependent actin filament-severing protein","volume":"9","author":"Lemaire","year":"1990","journal-title":"EMBO J."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1111\/j.1432-1033.1991.tb16051.x","article-title":"Different glycoforms of human thrombomodulin. Their glycosaminoglycan-dependent modulatory effects on thrombin inactivation by heparin cofactor II and antithrombin III","volume":"198","author":"Koyama","year":"1991","journal-title":"Eur. J. Biochem."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"6431","DOI":"10.1073\/pnas.82.19.6431","article-title":"Inhibition of chymotrypsin by heparin cofactor II","volume":"82","author":"Church","year":"1985","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"4751","DOI":"10.1021\/cr010170+","article-title":"Serpin structure, mechanism, and function","volume":"102","author":"Gettins","year":"2002","journal-title":"Chem. Rev."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1016\/j.ceca.2010.09.010","article-title":"RANKL-induced TRPV2 expression regulates osteoclastogenesis via calcium oscillations","volume":"48","author":"Kajiya","year":"2010","journal-title":"Cell Calcium"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"2543","DOI":"10.1083\/jcb.111.6.2543","article-title":"Osteoclast cytosolic calcium, regulated by voltage-gated calcium channels and extracellular calcium, controls podosome assembly and bone resorption","volume":"111","author":"Miyauchi","year":"1990","journal-title":"J. Cell Biol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"13719","DOI":"10.1073\/pnas.0812383106","article-title":"The crystal structure of the C-terminus of adseverin reveals the actin-binding interface","volume":"106","author":"Chumnarnsilpa","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"}],"container-title":["Cells"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2073-4409\/15\/17\/1607\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,10]],"date-time":"2026-09-10T04:24:28Z","timestamp":1789014268000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2073-4409\/15\/17\/1607"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9,3]]},"references-count":51,"journal-issue":{"issue":"17","published-online":{"date-parts":[[2026,9]]}},"alternative-id":["cells15171607"],"URL":"https:\/\/doi.org\/10.3390\/cells15171607","relation":{},"ISSN":["2073-4409"],"issn-type":[{"value":"2073-4409","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,9,3]]}}}