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glycob_cwt043.pdf | 4.57 MB | Adobe PDF | 見る/開く |
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dc.contributor.author | Nakagawa, Naoki | en |
dc.contributor.author | Takematsu, Hiromu | en |
dc.contributor.author | Oka, Shogo | en |
dc.contributor.alternative | 岡, 昌吾 | ja |
dc.date.accessioned | 2014-09-19T07:03:03Z | - |
dc.date.available | 2014-09-19T07:03:03Z | - |
dc.date.issued | 2013-09 | - |
dc.identifier.issn | 0959-6658 | - |
dc.identifier.uri | http://hdl.handle.net/2433/189744 | - |
dc.description.abstract | Dystroglycan (DG) is a cell surface glycoprotein that connects extracellular matrix molecules to the intracellular cytoskeleton, functioning as mechanical and signaling axes in various physiological events. Since the ligand-binding activity of DG strictly depends on O-mannosyl glycans attached to its extracellular α-DG subunit, aberrant glycosylation causes dystroglycanopathy, a subclass of congenital muscular dystrophy. Accumulating evidence shows that like-acetylglucosaminyltransferase (LARGE), a glycosyltransferase involved in the biosynthesis of a phosphodiester-linked modification on O-mannose, is essential for α-DG to gain the ligand-binding activity. We previously reported that human natural killer-1 sulfotransferase (HNK-1ST), which was originally reported as one of the enzymes responsible for HNK-1 glycoepitope, had an ability to suppress the glycosylation and the function of α-DG. In this study, we investigated how HNK-1ST regulates the glycosylation of α-DG using deletion and mutation analyses. We generated an α-DG mutant which has only one threonine residue capable of being modified by LARGE. Focusing on the single post-phosphoryl modification site, we found that HNK-1ST showed an almost complete inhibition of the LARGE-dependent modification and transferred a sulfate group to the phosphodiester-linked moiety on O-mannose. Furthermore, using an in vitro enzymatic assay system, we demonstrated that the sulfated α-DG by HNK-1ST is no longer glycosylated by LARGE. These results illustrate one possible glycosylation pathway where α-DG function is regulated by opposing actions of HNK-1ST and LARGE. | en |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | Oxford University Press | en |
dc.rights | This is a pre-copyedited, author-produced PDF of an article accepted for publication in "Glycobiology" following peer review. The version of record "Naoki Nakagawa, Hiromu Takematsu, and Shogo Oka; HNK-1 sulfotransferase-dependent sulfation regulating laminin-binding glycans occurs in the post-phosphoryl moiety on α-dystroglycan; Glycobiology (2013) 23 (9): 1066-1074 first published online May 30, 2013 doi:10.1093/glycob/cwt043" is available online at: http://glycob.oxfordjournals.org/content/23/9/1066 | en |
dc.rights | This is not the published version. Please cite only the published version. | en |
dc.rights | この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。 | ja |
dc.subject | α-dystroglycan | en |
dc.subject | HNK-1ST | en |
dc.subject | laminin-binding glycan | en |
dc.subject | LARGE | en |
dc.subject | sulfation | en |
dc.title | HNK-1 sulfotransferase-dependent sulfation regulating laminin-binding glycans occurs in the post-phosphoryl moiety on α-dystroglycan. | en |
dc.type | journal article | - |
dc.type.niitype | Journal Article | - |
dc.identifier.ncid | AA10826501 | - |
dc.identifier.jtitle | Glycobiology | en |
dc.identifier.volume | 23 | - |
dc.identifier.issue | 9 | - |
dc.identifier.spage | 1066 | - |
dc.identifier.epage | 1074 | - |
dc.relation.doi | 10.1093/glycob/cwt043 | - |
dc.textversion | author | - |
dc.identifier.pmid | 23723439 | - |
dcterms.accessRights | open access | - |
出現コレクション: | 学術雑誌掲載論文等 |
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