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NMDA receptor activation requires remodelling of intersubunit contacts within ligand-binding heterodimers

In non-NMDA glutamate receptors, intersubunit contacts within agonist binding domains affect functional desensitization. Now, NMDA receptor activation, but not desensitization, is shown to involve rearrangements at the heterodimer interface, suggesting that the intersubunit contacts of NMDA and non-NMDA receptors may have distinct functional roles.

William F. Borschel
Swetha E. Murthy
Gabriela K. Popescu
Research11 Oct 2011
Nature Communications

Volume: 2, P: 1-6
Correction: Corrigendum: Dehydrated hereditary stomatocytosis linked to gain-of-function mutations in mechanically activated PIEZO1 ion channels

Juliette Albuisson
Swetha E. Murthy
Ardem Patapoutian
Amendments and Corrections23 Sept 2013
Nature Communications

Volume: 4, P: 1
Dehydrated hereditary stomatocytosis linked to gain-of-function mutations in mechanically activated PIEZO1 ion channels

Dehydrated hereditary stomatocytosis is a genetic condition in which the permeability of red blood cells to cations in increased. Albuisson and colleagues find that mutations in the mechanically-activated PIEZO1 ion channel are the major cause of the disease and result in more slowly inactivating currents.

Juliette Albuisson
Swetha E Murthy
Ardem Patapoutian
Research21 May 2013
Nature Communications

Volume: 4, P: 1-9
Author Correction: Structure of the mechanically activated ion channel Piezo1

Kei Saotome
Swetha E. Murthy
Andrew B. Ward
Amendments and Corrections04 Jul 2022
Nature

Volume: 607, P: E10
Piezo1 ion channel pore properties are dictated by C-terminal region

Piezo ion channels function as mechanotransducers involved in vascular development and touch sensing, but their structural features remain unknown. Here the authors find that the C-terminal region of Piezo protein encompasses the pore and identify a glutamate residue within this region involved in ion conduction properties.

Bertrand Coste
Swetha E. Murthy
Ardem Patapoutian
ResearchOpen Access26 May 2015
Nature Communications

Volume: 6, P: 1-11
Structural insights into the Venus flytrap mechanosensitive ion channel Flycatcher1

Flycatcher1 (FLYC1) is a candidate mechanosensitive channel involved in Venus flytrap touch-induced prey capture. Here, the authors report structural and functional details of FLYC1, with insights into gating conformational transitions.

Sebastian Jojoa-Cruz
Kei Saotome
Andrew B. Ward
ResearchOpen Access14 Feb 2022
Nature Communications

Volume: 13, P: 1-11
Structure of the mechanically activated ion channel Piezo1

The cryo-electron microscopy structure of full-length mouse Piezo1 reveals six Piezo repeats, and 26 transmembrane helices per protomer, and shows that a kinked helical beam and anchor domain link the Piezo repeats to the pore and control gating allosterically.

Kei Saotome
Swetha E. Murthy
Andrew B. Ward
Research20 Dec 2017
Nature

Volume: 554, P: 481-486
Piezos thrive under pressure: mechanically activated ion channels in health and disease

Soon after their discovery in 2010, Piezo channels became a paradigm for studying mechanosensitive ion channels. These channels respond to physiologically relevant forces in diverse cellular contexts, and their dysfunction has been linked to various diseases. We are now starting to understand gating mechanisms of Piezo channels and their key roles in physiology.

Swetha E. Murthy
Adrienne E. Dubin
Ardem Patapoutian
Reviews04 Oct 2017
Nature Reviews Molecular Cell Biology

Volume: 18, P: 771-783

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