Multispanning membrane protein SIDT2 increases knockdown activity of gapmer antisense oligonucleotides.

ABSTRACT: Recent advances in the clinical development of oligonucleotide therapeutics, such as antisense oligonucleotides (ASOs) and small interfering RNAs, have attracted attention as promising therapeutic modalities for genetic and intractable diseases. These oligonucleotide therapeutics exert their efficacy by binding to target RNAs present within cells; however, the mechanisms underlying their cellular uptake, especially their passage through membranes, remain largely unclear. In the nematode, Caenorhabditis elegans, the multi-pass transmembrane protein, SID-1, is involved in the cellular uptake of double-stranded RNAs. In mammals, SIDT1 and SIDT2 (SID-1 transmembrane family, members 1 and 2, respectively) are homologs of SID-1, yet their functional differences are not fully understood. In this

SUBMITTER: Kusumoto K 

PROVIDER: S-EPMC11696054 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature