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Updated: Jan 21, 2026

Determination of In Vitro and Cellular Turn-on Kinetics for Fluorogenic RNA Aptamers
Published on: August 9, 2022
Identification of RNA aptamer which specifically interacts with PtdIns(3)P
Thoria Donia1, Bala Jyoti2, Futoshi Suizu3
1Division of Cancer Biology, Institute for Genetic Medicine, Hokkaido University, Sapporo, Japan; Chemistry Department, Faculty of Science, Tanta University, Egypt.
Abstract:
The phosphinositide PtdIns(3)P plays an important role in autophagy; however, the detailed mechanism of its activity remains unclear. Here, we used a Systematic Evolution of Ligands by EXponential enrichment (SELEX) screening approach to identify an RNA aptamer of 40 nucleotides that specifically recognizes and binds to intracellular lysosomal PtdIns(3)P. Binding occurs in a magnesium concentration- and pH-dependent manner, and consequently inhibits autophagy as determined by LC3II/I conversion, p62 degradation, formation of LC3 puncta, and lysosomal accumulation of Phafin2. These effects in turn inhibited lysosomal acidification, and the subsequent hydrolytic activity of cathepsin D following induction of autophagy. Given the essential role of PtdIns(3)P as a key targeting molecule for autophagy induction, identification of this novel PtdIns(3)P RNA aptamer provides new opportunities for investigating the biological functions and mechanisms of phosphoinositides.
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