%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.