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Mammalian cell function is dynamically regulated by the interaction of cell surface galectins with branched N-glycans. Here we report that N-glycan branching deficiency triggers the Golgi to generate bioequivalent N-glycans that preserve galectin-glycoprotein interactions and cellular homeostasis. Galectins bind N-acetyllactosamine (LacNAc) units within N-glycans initiated from UDP-GlcNAc by the medial-Golgi branching enzymes as well as the trans-Golgi poly-LacNAc extension enzyme \u03b21,3-N-acetylglucosaminyltransferase (B3GNT). Marginally reducing LacNAc content by limiting N-glycans to three branches results in T-cell hyperactivity and autoimmunity; yet further restricting branching does not produce a more hyperactive state. Rather, new poly-LacNAc extension by B3GNT maintains galectin binding and immune homeostasis. Poly-LacNAc extension is triggered by redistribution of unused UDP-GlcNAc from the medial to trans-Golgi via inter-cisternal tubules. These data demonstrate the functional equivalency of structurally dissimilar N-glycans and suggest a self-correcting feature of the Golgi that sustains cellular homeostasis.<\/jats:p>","DOI":"10.7554\/elife.14814","type":"journal-article","created":{"date-parts":[[2016,6,8]],"date-time":"2016-06-08T08:33:35Z","timestamp":1465374815000},"source":"Crossref","is-referenced-by-count":84,"title":["Golgi self-correction generates bioequivalent glycans to preserve cellular homeostasis"],"prefix":"10.7554","volume":"5","author":[{"given":"Haik","family":"Mkhikian","sequence":"first","affiliation":[{"name":"Department of Microbiology and Molecular Genetics, University of California, Irvine, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christie-Lynn","family":"Mortales","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Molecular Genetics, University of California, Irvine, United 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