Academic Journal
Demonstration of an oligosaccharide-diphosphodolichol diphosphatase activity whose subcellular localization is different than those of dolichyl-phosphate-dependent enzymes of the dolichol cycle
| العنوان: | Demonstration of an oligosaccharide-diphosphodolichol diphosphatase activity whose subcellular localization is different than those of dolichyl-phosphate-dependent enzymes of the dolichol cycle |
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| المؤلفون: | Massarweh, Ahmad, Bosco, Michaël, Iatmanen-Harbi, Soria, Tessier, Clarice, Auberger, Nicolas, Busca, Patricia, Chantret, Isabelle, Gravier-Pelletier, Christine, Moore, Stuart |
| المساهمون: | Centre de recherche sur l'Inflammation (CRI (UMR_S_1149 / ERL_8252 / U1149)), Université Paris Diderot - Paris 7 (UPD7)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Chimie et de Biochimie Pharmacologiques et Toxicologiques (LCBPT - UMR 8601), Université Paris Descartes - Paris 5 (UPD5)-Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS) |
| المصدر: | ISSN: 0022-2275 ; Journal of Lipid Research ; https://hal.science/hal-02997964 ; Journal of Lipid Research, 2016, 57 (6), pp.1029-1042. ⟨10.1194/jlr.M067330⟩. |
| بيانات النشر: | HAL CCSD American Society for Biochemistry and Molecular Biology |
| سنة النشر: | 2016 |
| مصطلحات موضوعية: | oligosaccharide-diphosphodolichol, endoplasmic reticulum, Golgi apparatus, isoprenoids, phosphatases, phospholipids/trafficking, N-linked glycosylation, dolichol-linked oligosaccharide, oligosaccharide-diphosphodolichol diphosphatase, EC 3.6.1.44, oligosaccharyl phosphates, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM] |
| الوصف: | International audience ; Oligosaccharyl phosphates (OSPs) are hydrolyzed from oligosaccharide-diphosphodolichol (DLO) during protein N-glycosylation by an uncharacterized process. An OSP-generating activity has been reported in vitro, and here we asked if its biochemical characteristics are compatible with a role in endoplasmic reticulum (ER)-situated DLO regulation. We demonstrate a Co2+-dependent DLO diphosphatase (DLODP) activity that splits DLO into dolichyl phosphate and OSP. DLODP has a pH optimum of 5.5 and is inhibited by vanadate but not by NaF. Polyprenyl diphosphates inhibit [3H]OSP release from [3H]DLO, the length of their alkyl chains correlating positively with inhibition potency. The diphosphodiester GlcNAc2-PP-solanesol is hydrolyzed to yield GlcNAc2-P and inhibits [3H]OSP release from [3H]DLO more effectively than the diphosphomonoester solanesyl diphosphate. During subcellular fractionation of liver homogenates, DLODP codistributes with microsomal markers, and density gradient centrifugation revealed that the distribution of DLODP is closer to that of Golgi apparatus-situated UDP-galactose glycoprotein galactosyltransferase than those of dolichyl-P-dependent glycosyltransferases required for DLO biosynthesis in the ER. Therefore, a DLODP activity showing selectivity toward lipophilic diphosphodiesters such as DLO, and possessing properties distinct from other lipid phosphatases, is identified. Separate subcellular locations for DLODP action and DLO biosynthesis may be required to prevent uncontrolled DLO destruction |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| Relation: | hal-02997964; https://hal.science/hal-02997964; https://hal.science/hal-02997964/document; https://hal.science/hal-02997964/file/PIIS0022227520351804.pdf; PUBMEDCENTRAL: PMC4878187 |
| DOI: | 10.1194/jlr.M067330 |
| الاتاحة: | https://hal.science/hal-02997964 https://hal.science/hal-02997964/document https://hal.science/hal-02997964/file/PIIS0022227520351804.pdf https://doi.org/10.1194/jlr.M067330 |
| Rights: | info:eu-repo/semantics/OpenAccess |
| رقم الانضمام: | edsbas.6A087724 |
| قاعدة البيانات: | BASE |
| DOI: | 10.1194/jlr.M067330 |
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