{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,31]],"date-time":"2026-07-31T20:08:13Z","timestamp":1785528493231,"version":"3.56.0"},"reference-count":106,"publisher":"Oxford University Press (OUP)","issue":"9","license":[{"start":{"date-parts":[[2026,7,31]],"date-time":"2026-07-31T00:00:00Z","timestamp":1785456000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/pages\/standard-publication-reuse-rights"}],"funder":[{"name":"Grant-in-Aid for Scientific Research","award":["25\u00a0K10718"],"award-info":[{"award-number":["25\u00a0K10718"]}]},{"name":"Grant-in-Aid for Scientific Research","award":["23\u00a0K27133"],"award-info":[{"award-number":["23\u00a0K27133"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,7,31]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Glycosylation is a common post-translational modification in mammalian cells. Abnormal glycosylation is a universal feature of cancer cells, regarded as a hallmark of cancer, and can influence tumor progression, including cell adhesion, migration, growth, differentiation, and invasion. A key change in N-glycosylation involves the modification of bisecting N-acetylglucosamine (GlcNAc), which is catalyzed by N-acetylglucosaminyltransferase III (GnT-III, encoded by the MGAT3 gene). GnT-III is widely regarded as a key glycosyltransferase in N-glycan biosynthesis. The addition of a bisecting GlcNAc prevents further processing of N-glycans, thereby blocking the synthesis of GlcNAc-branched N-glycans by N-acetylglucosaminyltransferase IV (GnT-IV) and N-acetylglucosaminyltransferase V (GnT-V). These branched N-glycans are strongly associated with cancer invasion and metastasis. For example, in many cases, integrins and E-cadherin are modified by GnT-V, which promotes cell migration and cancer invasion. In contrast, those modified by GnT-III tend to inhibit cell migration and metastasis. Recent studies also show that GnT-III expression suppresses cancer chemoresistance caused by prolonged exposure to anticancer drugs and enhances the differentiation capacity of leukemia cells. This review will discuss the roles of GnT-III in cancer cell behavior and cellular signaling, with a particular focus on some potential target proteins.<\/jats:p>","DOI":"10.1093\/glycob\/cwaf058","type":"journal-article","created":{"date-parts":[[2025,9,24]],"date-time":"2025-09-24T12:23:51Z","timestamp":1758716631000},"source":"Crossref","is-referenced-by-count":1,"title":["Revisiting the roles of N-acetylglucosaminyltransferase III (GnT-III\/MGAT3) in cancer cell behavior and cellular signaling"],"prefix":"10.1093","volume":"36","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-0241-8788","authenticated-orcid":false,"given":"Jianguo","family":"Gu","sequence":"first","affiliation":[{"name":"Division of Regulatory Glycobiology, Graduate School of Pharmaceutical Sciences , Tohoku Medical and Pharmaceutical University, 4-4-1 Komatsushima, Aoba-ku, Sendai, Miyagi 981-8558,","place":["Japan"]},{"name":"Division of Regulatory Glycobiology, Institute of Molecular Biomembrane and Glycobiology, Tohoku Medical and Pharmaceutical University , 4-4-1 Komatsushima, Aoba-ku, Sendai, Miyagi 981-8558 ,","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2026,7,31]]},"reference":[{"key":"2026073104421012100_ref1","doi-asserted-by":"publisher","first-page":"3221","DOI":"10.1002\/pmic.200800038","article-title":"N-acetylglucosaminyltransferase III expression is regulated by cell-cell adhesion via the E-cadherin\u2013catenin\u2013actin complex","volume":"8","author":"Akama","year":"2008","journal-title":"Proteomics"},{"key":"2026073104421012100_ref2","doi-asserted-by":"publisher","first-page":"2213","DOI":"10.1074\/mcp.M113.037085","article-title":"Specific glycosylation of membrane proteins in epithelial ovarian cancer cell lines: glycan structures reflect gene expression and DNA methylation status","volume":"13","author":"Anugraham","year":"2014","journal-title":"Mol Cell Proteomics: 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