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Tytuł:
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Involvement of LH3 and GLT25D1 for glucosyl-galactosyl-hydroxylation on non-collagen-like domain of FGL1.
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Autorzy:
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Mori K; Department of Applied Chemistry, Faculty of Science and Technology, Keio University, Yokohama, 223-8522, Japan.
Suzuki T; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Wako, 351-0198, Japan.
Miura K; Department of Applied Chemistry, Faculty of Science and Technology, Keio University, Yokohama, 223-8522, Japan.
Dohmae N; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Wako, 351-0198, Japan.
Simizu S; Department of Applied Chemistry, Faculty of Science and Technology, Keio University, Yokohama, 223-8522, Japan. Electronic address: .
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Źródło:
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Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2021 Jun 30; Vol. 560, pp. 93-98. Date of Electronic Publication: 2021 May 10.
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Typ publikacji:
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Journal Article; Research Support, Non-U.S. Gov't
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Język:
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English
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Imprint Name(s):
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Publication: <2002- >: San Diego, CA : Elsevier
Original Publication: New York, Academic Press.
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MeSH Terms:
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Fibrinogen/*metabolism
Galactosyltransferases/*metabolism
Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase/*metabolism
Cell Line, Tumor ; Fibrinogen/chemistry ; Glycosylation ; Humans ; Lysine/metabolism ; Protein Domains ; Protein Processing, Post-Translational ; Protein Stability
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Contributed Indexing:
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Keywords: FGL1; GLT25D1; Glucosyl-galactosyl-hydroxylation; LH3; Mass spectrometry
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Substance Nomenclature:
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0 (FGL1 protein, human)
9001-32-5 (Fibrinogen)
EC 1.14.11.- (PLOD3 protein, human)
EC 1.14.11.4 (Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase)
EC 2.4.1.- (Galactosyltransferases)
EC 2.4.1.50 (COLGALT1 protein, human)
K3Z4F929H6 (Lysine)
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Entry Date(s):
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Date Created: 20210513 Date Completed: 20210826 Latest Revision: 20211026
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Update Code:
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20240105
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DOI:
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10.1016/j.bbrc.2021.04.128
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PMID:
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33984770
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Glucosyl-galactosyl-hydroxylation (GGH) is one type of post-translational modification, which is mainly observed in collagen-like domain-containing proteins. Using LC-MS/MS analysis, we found a GGH-like modification at Lys65 of fibrinogen-like protein 1 (FGL1), although it does not contain a collagen-like domain. To identify the glycosyltransferases responsible for this modification, we established LH3/GLT25D1-knockout FGL1-overexpressing HT1080 cell lines. The result showed that knockout of LH3 or GLT25D1 significantly inhibited the glycosylation. Furthermore, deficiency of GGH by point mutation of the FGL1 protein or knockout of the GGH-related glycosyltransferase reduced FGL1 protein levels. Taken together, these data indicate that Lys65 of FGL1 is glucosyl-galactosyl-hydroxylated by LH3 and GLT25D1. Our results provide novel insights to regulate various FGL1 functions.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2021 Elsevier Inc. All rights reserved.)
