TY - JOUR
T1 - Author Correction
T2 - Structure of the mechanically activated ion channel Piezo1 (Nature, (2018), 554, 7693, (481-486), 10.1038/nature25453)
AU - Saotome, Kei
AU - Murthy, Swetha E.
AU - Kefauver, Jennifer M.
AU - Whitwam, Tess
AU - Patapoutian, Ardem
AU - Ward, Andrew B.
N1 - Publisher Copyright:
© 2022, The Author(s), under exclusive licence to Springer Nature Limited.
PY - 2022/7/21
Y1 - 2022/7/21
N2 - In this Article, we highlighted important residues that could affect Piezo1 gating. Accordingly, in Fig. 3 and Extended Data Fig. 7 of the Article, we measured mechanically activated currents from cells that express alanine substitution mutants (M2493A and F2494A) of residues that we predicted as the hydrophobic gate of the channel. Our experiments showed that the single mutants cause a gain-of-function phenotype (Fig. 3g–i). As a control, we also tested the double mutant M2493A/F2494A, which we found to be non-functional (Extended Data Fig. 7a,b).
AB - In this Article, we highlighted important residues that could affect Piezo1 gating. Accordingly, in Fig. 3 and Extended Data Fig. 7 of the Article, we measured mechanically activated currents from cells that express alanine substitution mutants (M2493A and F2494A) of residues that we predicted as the hydrophobic gate of the channel. Our experiments showed that the single mutants cause a gain-of-function phenotype (Fig. 3g–i). As a control, we also tested the double mutant M2493A/F2494A, which we found to be non-functional (Extended Data Fig. 7a,b).
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U2 - 10.1038/s41586-022-04976-8
DO - 10.1038/s41586-022-04976-8
M3 - Comment/debate
C2 - 35788193
AN - SCOPUS:85133307992
SN - 0028-0836
VL - 607
SP - E10
JO - Nature
JF - Nature
IS - 7919
ER -