2022
DOI: 10.1016/j.jbc.2021.101487
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Cryo-EM structure of mouse TRPML2 in lipid nanodiscs

Abstract: This is a PDF file of an article that has undergone enhancements after acceptance, such as the addition of a cover page and metadata, and formatting for readability, but it is not yet the definitive version of record. This version will undergo additional copyediting, typesetting and review before it is published in its final form, but we are providing this version to give early visibility of the article. Please note that, during the production process, errors may be discovered which could affect the content, a… Show more

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Cited by 6 publications
(2 citation statements)
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“…The TOP domain sits on the extracellular side of the VSD, extending from the S1 and S2 helices to form extracellular contacts with the S3-S4 loop (Figures 1a and 2a). Although this protein fold is unique to polycystins, it is structurally similar to the extraluminal domain of the lysosomal mucolipin TRP channels (48,49).…”
Section: Top Domainmentioning
confidence: 99%
“…The TOP domain sits on the extracellular side of the VSD, extending from the S1 and S2 helices to form extracellular contacts with the S3-S4 loop (Figures 1a and 2a). Although this protein fold is unique to polycystins, it is structurally similar to the extraluminal domain of the lysosomal mucolipin TRP channels (48,49).…”
Section: Top Domainmentioning
confidence: 99%
“…High-resolution structures of TPCs and TRPMLs have been obtained by cryo-EM in recent years (Fig. 1) (Dickinson et al, 2020;Fine et al, 2018;She et al, 2018She et al, , 2019Song et al, 2022;Zhou et al, 2017). This has provided novel molecular insights into channel regulation by stimuli such as PI(3,5)P 2 and voltage.…”
Section: Introductionmentioning
confidence: 99%