%0 Journal Article %@ 0143-4160 %A Rahman, Taufiq %A Patel, Sandip %D 2022 %F discovery:10150239 %I ELSEVIER SCI LTD %J Cell Calcium %K Science & Technology, Life Sciences & Biomedicine, Cell Biology, TRPML1, PI(3,5)P-2, Rapamycin, Allosteric, Temsirolimus, Lysosome, Ca2+ channels %T Rendezvous with PI(3,5)P-2-A rapalog gets caught opening TRPML1 %U https://discovery-pp.ucl.ac.uk/id/eprint/10150239/ %V 105 %X TRPML1 is an endolysosomally-expressed cation channel, activated physiologically by PI(3,5)P2 and by several synthetic agonists including rapamycin. New high resolution cryo-EM- structures of TRPML1 bound to both PI(3,5)P2 and temsirolimus - a rapamycin analog provides molecular insight into how the channel integrates two agonists that bind to distal sites but act cooperatively. %Z This version is the author accepted manuscript. For information on re-use, please refer to the publisher's terms and conditions.