Characterization of N-glycosylation and its functional role in SIDT1-Mediated RNA uptake
Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved..
The mammalian SID-1 transmembrane family members, SIDT1 and SIDT2, are multipass transmembrane proteins that mediate the cellular uptake and intracellular trafficking of nucleic acids, playing important roles in the immune response and tumorigenesis. Previous work has suggested that human SIDT1 and SIDT2 are N-glycosylated, but the precise site-specific N-glycosylation information and its functional contribution remain unclear. In this study, we use high-resolution liquid chromatography tandem mass spectrometry to comprehensively map the N-glycosites and quantify the N-glycosylation profiles of SIDT1 and SIDT2. Further molecular mechanistic probing elucidates the essential role of N-linked glycans in regulating cell surface expression, RNA binding, protein stability, and RNA uptake of SIDT1. Our results provide crucial information about the potential functional impact of N-glycosylation in the regulation of SIDT1-mediated RNA uptake and provide insights into the molecular mechanisms of this promising nucleic acid delivery system with potential implications for therapeutic applications.
Medienart: |
E-Artikel |
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Erscheinungsjahr: |
2024 |
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Erschienen: |
2024 |
Enthalten in: |
Zur Gesamtaufnahme - volume:300 |
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Enthalten in: |
The Journal of biological chemistry - 300(2024), 2 vom: 01. Feb., Seite 105654 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Yang, Tingting [VerfasserIn] |
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Links: |
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Anmerkungen: |
Date Completed 26.02.2024 Date Revised 06.03.2024 published: Print-Electronic Citation Status MEDLINE |
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doi: |
10.1016/j.jbc.2024.105654 |
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funding: |
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Förderinstitution / Projekttitel: |
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PPN (Katalog-ID): |
NLM367281856 |
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520 | |a Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved. | ||
520 | |a The mammalian SID-1 transmembrane family members, SIDT1 and SIDT2, are multipass transmembrane proteins that mediate the cellular uptake and intracellular trafficking of nucleic acids, playing important roles in the immune response and tumorigenesis. Previous work has suggested that human SIDT1 and SIDT2 are N-glycosylated, but the precise site-specific N-glycosylation information and its functional contribution remain unclear. In this study, we use high-resolution liquid chromatography tandem mass spectrometry to comprehensively map the N-glycosites and quantify the N-glycosylation profiles of SIDT1 and SIDT2. Further molecular mechanistic probing elucidates the essential role of N-linked glycans in regulating cell surface expression, RNA binding, protein stability, and RNA uptake of SIDT1. Our results provide crucial information about the potential functional impact of N-glycosylation in the regulation of SIDT1-mediated RNA uptake and provide insights into the molecular mechanisms of this promising nucleic acid delivery system with potential implications for therapeutic applications | ||
650 | 4 | |a Journal Article | |
650 | 4 | |a N-glycosylation | |
650 | 4 | |a RNA transport | |
650 | 4 | |a SIDT1 | |
650 | 4 | |a SIDT2 | |
650 | 4 | |a intracellular localization of proteins | |
650 | 4 | |a mammalian SID-1 transmembrane family | |
650 | 4 | |a protein stability | |
650 | 7 | |a Membrane Proteins |2 NLM | |
650 | 7 | |a Nucleotide Transport Proteins |2 NLM | |
650 | 7 | |a RNA |2 NLM | |
650 | 7 | |a 63231-63-0 |2 NLM | |
650 | 7 | |a SIDT2 protein, human |2 NLM | |
650 | 7 | |a systemic RNA Interference-defective-1 transmembrane family member 1, human |2 NLM | |
700 | 1 | |a Xiao, Haonan |e verfasserin |4 aut | |
700 | 1 | |a Chen, Xiulan |e verfasserin |4 aut | |
700 | 1 | |a Zheng, Le |e verfasserin |4 aut | |
700 | 1 | |a Guo, Hangtian |e verfasserin |4 aut | |
700 | 1 | |a Wang, Jiaqi |e verfasserin |4 aut | |
700 | 1 | |a Jiang, Xiaohong |e verfasserin |4 aut | |
700 | 1 | |a Zhang, Chen-Yu |e verfasserin |4 aut | |
700 | 1 | |a Yang, Fuquan |e verfasserin |4 aut | |
700 | 1 | |a Ji, Xiaoyun |e verfasserin |4 aut | |
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