{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T14:42:44Z","timestamp":1791297764960,"version":"4.1.0"},"reference-count":0,"publisher":"Rockefeller University Press","issue":"5","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1989,11,1]]},"abstract":"<jats:p>Two CHO glycosylation mutants that were previously shown to lack N-linked carbohydrates with GlcNAc beta 1,6Man alpha 1,6 branches, and to belong to the same genetic complementation group, are shown here to differ in the activity of N-acetylglucosaminyltransferase V (GlcNAc-TV) (UDP-GlcNA: alpha 1,6mannose beta-N-acetylglucosaminyltransferase V). One mutant, Lec4, has no detectable GlcNAc-TV activity whereas the other, now termed Lec4A, has activity equivalent to that of parental CHO in detergent cell extracts. However, Lec4A GlcNAc-TV can be distinguished from CHO GlcNAc-TV on the basis of its increased sensitivity to heat inactivation and its altered subcellular compartmentalization. Sucrose density gradient fractionation shows that the major portion of GlcNAc-TV from Lec4A cells cofractionates with membranes of the ER instead of Golgi membranes where GlcNAc-TV is localized in parental CHO cells. Other experiments show that Lec4A GlcNAc-TV is not concentrated in lysosomes, or in a post-Golgi compartment, or at the cell surface. The altered localization in Lec4A cells is specific for GlcNAc-TV because two other Lec4A Golgi transferases cofractionate at the density of Golgi membranes. The combined data suggest that both lec4 and lec4A mutations affect the structural gene for GlcNAc-TV, causing either the loss of GlcNAc-TV activity (lec4) or its miscompartmentalization (lec4A). The identification of the Lec4A defect indicates that appropriate screening of different glycosylation-defective mutants should enable the isolation of other mammalian cell trafficking mutants.<\/jats:p>","DOI":"10.1083\/jcb.109.5.2089","type":"journal-article","created":{"date-parts":[[2004,5,15]],"date-time":"2004-05-15T00:18:20Z","timestamp":1084580300000},"page":"2089-2096","update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":46,"title":["The Lec4A CHO glycosylation mutant arises from miscompartmentalization of a Golgi glycosyltransferase."],"prefix":"10.1083","volume":"109","author":[{"given":"W","family":"Chaney","sequence":"first","affiliation":[{"name":"Department of Cell Biology, Albert Einstein College of Medicine, Bronx, NY 10461."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"S","family":"Sundaram","sequence":"additional","affiliation":[{"name":"Department of Cell Biology, Albert Einstein College of Medicine, Bronx, NY 10461."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"N","family":"Friedman","sequence":"additional","affiliation":[{"name":"Department of Cell Biology, Albert Einstein College of Medicine, Bronx, NY 10461."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"P","family":"Stanley","sequence":"additional","affiliation":[{"name":"Department of Cell Biology, Albert Einstein College of Medicine, Bronx, NY 10461."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"291","published-online":{"date-parts":[[1989,11,1]]},"container-title":["The Journal of cell biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/rupress.org\/jcb\/article-pdf\/109\/5\/2089\/1462724\/2089.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/rupress.org\/jcb\/article-pdf\/109\/5\/2089\/1462724\/2089.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,7,22]],"date-time":"2023-07-22T00:54:36Z","timestamp":1689987276000},"score":1,"resource":{"primary":{"URL":"https:\/\/rupress.org\/jcb\/article\/109\/5\/2089\/55777\/The-Lec4A-CHO-glycosylation-mutant-arises-from"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1989,11,1]]},"references-count":0,"journal-issue":{"issue":"5","published-print":{"date-parts":[[1989,11,1]]}},"URL":"https:\/\/doi.org\/10.1083\/jcb.109.5.2089","relation":{},"ISSN":["0021-9525","1540-8140"],"issn-type":[{"value":"0021-9525","type":"print"},{"value":"1540-8140","type":"electronic"}],"subject":[],"published":{"date-parts":[[1989,11,1]]}}}