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タイトル: | HNK-1 sulfotransferase-dependent sulfation regulating laminin-binding glycans occurs in the post-phosphoryl moiety on α-dystroglycan. |
著者: | Nakagawa, Naoki Takematsu, Hiromu Oka, Shogo |
著者名の別形: | 岡, 昌吾 |
キーワード: | α-dystroglycan HNK-1ST laminin-binding glycan LARGE sulfation |
発行日: | Sep-2013 |
出版者: | Oxford University Press |
誌名: | Glycobiology |
巻: | 23 |
号: | 9 |
開始ページ: | 1066 |
終了ページ: | 1074 |
抄録: | 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. |
著作権等: | 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 This is not the published version. Please cite only the published version. 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。 |
URI: | http://hdl.handle.net/2433/189744 |
DOI(出版社版): | 10.1093/glycob/cwt043 |
PubMed ID: | 23723439 |
出現コレクション: | 学術雑誌掲載論文等 |
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