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However, the molecular mechanisms underlying these processes remain poorly understood. This study identifies the vacuolar-type H\n                    <jats:sup>+<\/jats:sup>\n                    -ATPase (V-ATPase) a3 subunit as a key regulator of enamel formation via its role in secretory lysosome trafficking. In a3 knockout (a3KO) mice and cultured ameloblasts, a3 is required for both lysosomal acidification and the directional transport of odontogenic ameloblast-associated protein (ODAM)\u2013containing secretory lysosomes to the ruffled border membrane of M-ABs. At this site, ODAM is crucial for mediating ameloblast adhesion to the enamel matrix. Loss of a3 caused severe enamel hypomineralization, characterized by reduced matrix acidification, cystic enamel defects, abnormal ruffled border morphology, and ameloblast detachment from the mineralizing surface. In vitro, a3-deficient ameloblasts exhibited significantly impaired adhesion to hydroxyapatite, decreased ODAM expression, and suppressed lysosomal acidification, indicating a3 is functionally required for maintaining ameloblast function and polarity. Mechanistically, Rab27A served as an important adaptor linking a3-positive secretory lysosomes to the microtubule network, enabling their polarized movement toward the distal plasma membrane. Disruption of this a3\u2013Rab27A axis in a3KO cells mislocalized secretory lysosomes and defective ODAM delivery into the enamel matrix, compromising enamel mineralization. These findings reveal a new mechanism by which a3 orchestrates lysosomal positioning and ODAM secretion in enamel-forming cells. By integrating proton transport with vesicular trafficking and adhesion protein delivery, a3 functions as a key regulator of enamel mineralization. This study provides new insights into the pathogenesis of enamel hypomineralization and identifies a3 and its associated pathways as potential therapeutic targets for treating developmental enamel defects.\n                  <\/jats:p>","DOI":"10.1177\/00220345251401512","type":"journal-article","created":{"date-parts":[[2026,1,21]],"date-time":"2026-01-21T12:16:29Z","timestamp":1768997789000},"page":"1195-1204","update-policy":"https:\/\/doi.org\/10.1177\/sage-journals-update-policy","source":"Crossref","is-referenced-by-count":0,"title":["V-ATPase a3 Directs Secretory Lysosome Transport in Enamel Formation"],"prefix":"10.1177","volume":"105","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-3954-9442","authenticated-orcid":false,"given":"K.","family":"Otsu","sequence":"first","affiliation":[{"name":"Division of Developmental Biology and Regenerative Medicine, Department of Anatomy, Iwate Medical University, Yahaba, Iwate, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"S.","family":"Ikezaki","sequence":"additional","affiliation":[{"name":"Division of Developmental Biology and Regenerative Medicine, Department of Anatomy, Iwate Medical University, Yahaba, Iwate, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"N.","family":"Goto-Matsumoto","sequence":"additional","affiliation":[{"name":"Center for Basic Medical Research, International University of Health and Welfare, Narita, Chiba, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"A.","family":"Ikarashi","sequence":"additional","affiliation":[{"name":"Division of Instrumental Analysis, Center for Coordination of Research Facilities, Institute for Research Administration, Niigata University, Chuo-ku, Niigata, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"H.","family":"Sano","sequence":"additional","affiliation":[{"name":"Department of Pathology, The Nippon Dental University School of Life Dentistry at Niigata, Chuo-ku, Niigata, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"H.","family":"Ida-Yonemochi","sequence":"additional","affiliation":[{"name":"Division of Anatomy and Cell Biology of the Hard Tissue, Department of Tissue Regeneration and Reconstruction, Niigata University Graduate School of Medical and Dental Sciences, Chuo-ku, Niigata, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8571-9900","authenticated-orcid":false,"given":"H.","family":"Ohshima","sequence":"additional","affiliation":[{"name":"Division of Anatomy and Cell Biology of the Hard Tissue, Department of Tissue Regeneration and Reconstruction, Niigata University Graduate School of Medical and Dental Sciences, Chuo-ku, Niigata, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"G.-H.","family":"Sun-Wada","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Faculty of Pharmaceutical Sciences, Doshisha Women\u2019s College, Kyotanabe, Kyoto, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Y.","family":"Wada","sequence":"additional","affiliation":[{"name":"Division of Biological Sciences, Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M.","family":"Nakanishi-Matsui","sequence":"additional","affiliation":[{"name":"Division of Biochemistry, School of Pharmacy, Iwate Medical University, Yahaba, Iwate, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9724-8568","authenticated-orcid":false,"given":"H.","family":"Harada","sequence":"additional","affiliation":[{"name":"Division of Developmental Biology and Regenerative Medicine, Department of Anatomy, Iwate Medical University, Yahaba, Iwate, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"179","published-online":{"date-parts":[[2026,1,21]]},"reference":[{"key":"e_1_3_3_2_1","doi-asserted-by":"crossref","unstructured":"Al Kawas S Amizuka N Bergeron JJ Warshawsky H. 1996. 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