Author Correction: Structure of the mechanically activated ion channel Piezo1 (original) (raw)
- Author Correction
- Published: 04 July 2022
- Swetha E. Murthy1,
- Jennifer M. Kefauver1,2,
- Tess Whitwam1,
- Ardem Patapoutian1 &
- …
- Andrew B. Ward2
Nature volume 607, page E10 (2022)Cite this article
- 2592 Accesses
- 11 Altmetric
- Metrics details
Correction to: Nature https://doi.org/10.1038/nature25453 Published online 20 December 2017
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).
Prompted by a recent request from a peer in the field, we re-sequenced the plasmid used for the M2493A/F2494A double mutant and found that there was a base-pair deletion immediately downstream of the mutagenesis site, resulting in a frameshift at the Piezo1 C terminus. We now think that the non-functionality of the channel arises from the frameshift and early truncation of the protein, and not from the double mutation. Indeed, Zheng et al.1 demonstrated that the M2493A/F2494A mutation in Piezo1 is functional and results in a gain-of-function phenotype, consistent with our single-mutation results (figure 1d in ref. 1). Therefore, Extended Data Fig. 7a,b in our Article is misleading owing to a mistake made when the original DNA sequencing was conducted. We re-sequenced the other plasmids used in Fig. 3 and Extended Data Fig. 7 of the Article and confirmed that they contain the correct mutations. The main conclusions from the mutagenesis experiments stated in the main text of our Article are not affected by this mistake, nor is the overarching purpose of the paper, which is to describe details of the Piezo1 channel structure. The original Article has not been corrected online
References
- Zheng, W., Gracheva, E. O. & Bagriantsev, S. N. A hydrophobic gate in the inner pore helix is the major determinant of inactivation in mechanosensitive Piezo channels. Elife 8, e44003 (2019).
Article Google Scholar
Author information
Authors and Affiliations
- Howard Hughes Medical Institute, Department of Neuroscience, The Scripps Research Institute, La Jolla, California, USA
Kei Saotome, Swetha E. Murthy, Jennifer M. Kefauver, Tess Whitwam & Ardem Patapoutian - Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, USA
Kei Saotome, Jennifer M. Kefauver & Andrew B. Ward
Authors
- Kei Saotome
You can also search for this author inPubMed Google Scholar - Swetha E. Murthy
You can also search for this author inPubMed Google Scholar - Jennifer M. Kefauver
You can also search for this author inPubMed Google Scholar - Tess Whitwam
You can also search for this author inPubMed Google Scholar - Ardem Patapoutian
You can also search for this author inPubMed Google Scholar - Andrew B. Ward
You can also search for this author inPubMed Google Scholar
Corresponding authors
Correspondence toArdem Patapoutian or Andrew B. Ward.
Rights and permissions
About this article
Cite this article
Saotome, K., Murthy, S.E., Kefauver, J.M. et al. Author Correction: Structure of the mechanically activated ion channel Piezo1.Nature 607, E10 (2022). https://doi.org/10.1038/s41586-022-04976-8
- Published: 04 July 2022
- Issue Date: 21 July 2022
- DOI: https://doi.org/10.1038/s41586-022-04976-8
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.