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Dysregulation of IFs causes a wide range of human diseases, including skin disorders, cardiomyopathies, lipodystrophy, and neuropathy. Despite this pathophysiological significance, how cells regulate IF structure, dynamics, and function remains poorly understood. Here, we show that site-specific modification of the prototypical IF protein vimentin with O-linked \u03b2-N-acetylglucosamine (O-GlcNAc) mediates its homotypic protein-protein interactions and is required in human cells for IF morphology and cell migration. In addition, we show that the intracellular pathogen Chlamydia trachomatis, which remodels the host IF cytoskeleton during infection, requires specific vimentin glycosylation sites and O-GlcNAc transferase activity to maintain its replicative niche. Our results provide new insight into the biochemical and cell biological functions of vimentin O-GlcNAcylation, and may have broad implications for our understanding of the regulation of IF proteins in general.<\/jats:p>","DOI":"10.7554\/elife.31807","type":"journal-article","created":{"date-parts":[[2018,3,7]],"date-time":"2018-03-07T11:07:05Z","timestamp":1520420825000},"source":"Crossref","is-referenced-by-count":80,"title":["Site-specific glycosylation regulates the form and function of the intermediate filament cytoskeleton"],"prefix":"10.7554","volume":"7","author":[{"given":"Heather J","family":"Tarbet","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Duke University School of Medicine, Durham, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lee","family":"Dolat","sequence":"additional","affiliation":[{"name":"Department of Molecular Genetics and Microbiology, Duke University School of Medicine, Durham, United 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H","family":"Valdivia","sequence":"additional","affiliation":[{"name":"Department of Molecular Genetics and Microbiology, Duke University School of Medicine, Durham, United States"},{"name":"Center for Host-Microbial Interactions, Duke University School of Medicine, Durham, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2729-4876","authenticated-orcid":true,"given":"Michael","family":"Boyce","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Duke University School of Medicine, Durham, United States"},{"name":"Center for Host-Microbial Interactions, Duke University School of Medicine, Durham, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"4374","published-online":{"date-parts":[[2018,3,7]]},"reference":[{"key":"bib1","doi-asserted-by":"publisher","first-page":"560","DOI":"10.1038\/323560a0","article-title":"The nuclear lamina is a meshwork of intermediate-type 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