Rahman, Taufiq;
Patel, Sandip;
(2022)
Rendezvous with PI(3,5)P-2-A rapalog gets caught opening TRPML1.
Cell Calcium
, 105
, Article 102597. 10.1016/j.ceca.2022.102597.
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Abstract
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.
| Type: | Article |
|---|---|
| Title: | Rendezvous with PI(3,5)P-2-A rapalog gets caught opening TRPML1 |
| Location: | Netherlands |
| Open access status: | An open access version is available from UCL Discovery |
| DOI: | 10.1016/j.ceca.2022.102597 |
| Publisher version: | https://doi.org/10.1016/j.ceca.2022.102597 |
| Language: | English |
| Additional information: | This version is the author accepted manuscript. For information on re-use, please refer to the publisher's terms and conditions. |
| Keywords: | Science & Technology, Life Sciences & Biomedicine, Cell Biology, TRPML1, PI(3,5)P-2, Rapamycin, Allosteric, Temsirolimus, Lysosome, Ca2+ channels |
| UCL classification: | UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Cell and Developmental Biology UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences UCL UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences |
| URI: | https://discovery-pp.ucl.ac.uk/id/eprint/10150239 |
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