<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Ghosh, Arpita</style></author><author><style face="normal" font="default" size="100%">Pandey, Satya Prakash</style></author><author><style face="normal" font="default" size="100%">Ansari, Asgar Hussain</style></author><author><style face="normal" font="default" size="100%">Sundar, Jennifer Seematti</style></author><author><style face="normal" font="default" size="100%">Singh, Praveen</style></author><author><style face="normal" font="default" size="100%">Khan, Yasmeen</style></author><author><style face="normal" font="default" size="100%">Ekka, Mary Krishna</style></author><author><style face="normal" font="default" size="100%">Chakraborty, Debojyoti</style></author><author><style face="normal" font="default" size="100%">Maiti, Souvik</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Alternative splicing modulation mediated by G-quadruplex structures in MALAT1 lncRNA</style></title><secondary-title><style face="normal" font="default" size="100%">Nucleic Acids Research</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2022</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JAN</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">50</style></volume><pages><style face="normal" font="default" size="100%">378-396</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">MALAT1, an abundant lncRNA specifically localized to nuclear speckles, regulates alternative-splicing (AS). The molecular basis of its role in AS remains poorly understood. Here, we report three conserved, thermodynamically stable, parallel RNAG-quadruplexes (rG4s) present in the 3' region of MALAT1 which regulates this function. Using rG4 domain-specific RNA-pull-down followed by mass-spectrometry, RNA-immuno-precipitation, and imaging, we demonstrate the rG4 dependent localization of Nucleolin (NCL) and Nucleophosmin (NPM) to nuclear speckles. Specific G-to-A mutations that abolish rG4 structures, result in the localization loss of both the proteins from speckles. Functionally, disruption of rG4 in MALAT1 phenocopies NCL knockdown resulting in altered pre-mRNA splicing of endogenous genes. These results reveal a central role of rG4s within the 3' region of MALAT1 orchestrating AS.</style></abstract><issue><style face="normal" font="default" size="100%">1</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">16.917</style></custom4></record></records></xml>