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• W4313237723 startingPage "108" @default.
• W4313237723 abstract "Phosphorothioate (PS)-modified antisense oligonucleotide (ASO) drugs enter cells through endocytic pathways where a majority are entrapped within membrane-bound endosomes and lysosomes, representing a limiting step for antisense activity. While late endosomes have been identified as a major site for productive PS-ASO release, how lysosomes regulate PS-ASO activity beyond macromolecule degradation remains not fully understood. In this study, we reported that SID1 transmembrane family, member 2 (SIDT2), a lysosome transmembrane protein, can robustly regulate PS-ASO activity. We showed that SIDT2 is required for the proper colocalization between PS-ASO and lysosomes, suggesting an important role of SIDT2 in the entrapment of PS-ASOs in lysosomes. Mechanistically, we revealed that SIDT2 regulates lysosome cellular location. Lysosome location is largely determined by its movement along microtubules. Interestingly, we also observed an enrichment of proteins involved in microtubule function among SIDT2-binding proteins, suggesting that SIDT2 regulates lysosome location via its interaction with microtubule-related proteins. Overall, our data suggest that lysosome protein SIDT2 inhibits PS-ASO activity potentially through its interaction with microtubule-related proteins to place lysosomes at perinuclear regions, thus, facilitating PS-ASO's localization to lysosomes for degradation." @default.
• W4313237723 created "2023-01-06" @default.
• W4313237723 creator A5023202514 @default.
• W4313237723 creator A5057622461 @default.
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• W4313237723 date "2023-04-01" @default.
• W4313237723 modified "2023-09-28" @default.
• W4313237723 title "SIDT2 Inhibits Phosphorothioate Antisense Oligonucleotide Activity by Regulating Cellular Localization of Lysosomes" @default.
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• W4313237723 doi "https://doi.org/10.1089/nat.2022.0055" @default.
• W4313237723 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36576400" @default.
• W4313237723 hasPublicationYear "2023" @default.
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