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dc.contributor.authorAhat, Erpan
dc.contributor.authorSong, Yuefan
dc.contributor.authorXia, Ke
dc.contributor.authorReid, Whitney
dc.contributor.authorLi, Jie
dc.contributor.authorBui, Sarah
dc.contributor.authorZhang, Fuming
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorWang, Yanzhuang
dc.date2022
dc.date.accessioned2022-06-23T03:26:40Z
dc.date.available2022-06-23T03:26:40Z
dc.date.issued2022-04-01
dc.identifier.citationGRASP depletion-mediated Golgi fragmentation impairs glycosaminoglycan synthesis, sulfation, and secretion, E. Ahat, Y. Song, K. Xia, W. Reid, J. Li, S. Bui, F. Zhang, R. J. Linhardt, Y. Wang, Cellular and Molecular Life Sciences, 79, 199, 2022.
dc.identifier.issn14209071
dc.identifier.issn1420682X
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5144
dc.identifier.urihttps://doi.org/10.1007/s00018-022-04223-3
dc.descriptionCellular and Molecular Life Sciences, 79, 199
dc.descriptionNote : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
dc.description.abstractSynthesis of glycosaminoglycans, such as heparan sulfate (HS) and chondroitin sulfate (CS), occurs in the lumen of the Golgi, but the relationship between Golgi structural integrity and glycosaminoglycan synthesis is not clear. In this study, we disrupted the Golgi structure by knocking out GRASP55 and GRASP65 and determined its effect on the synthesis, sulfation, and secretion of HS and CS. We found that GRASP depletion increased HS synthesis while decreasing CS synthesis in cells, altered HS and CS sulfation, and reduced both HS and CS secretion. Using proteomics, RNA-seq and biochemical approaches, we identified EXTL3, a key enzyme in the HS synthesis pathway, whose level is upregulated in GRASP knockout cells; while GalNAcT1, an essential CS synthesis enzyme, is robustly reduced. In addition, we found that GRASP depletion decreased HS sulfation via the reduction of PAPSS2, a bifunctional enzyme in HS sulfation. Our study provides the first evidence that Golgi structural defect may significantly alter the synthesis and secretion of glycosaminoglycans.
dc.description.sponsorshipNational Science Foundation
dc.languageen_US
dc.language.isoENG
dc.publisherSpringer
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofCellular and Molecular Life Sciences
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleGRASP depletion-mediated Golgi fragmentation impairs glycosaminoglycan synthesis, sulfation, and secretion
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1007/s00018-022-04223-3
dc.rights.holderIn Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/
dc.creator.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
rpi.description.volume79


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