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조회483

Vollum Institute, OHSU

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Proc. Natl. Acad. Sci. USA, Feb 20 2024, 121 (8) | https://doi.org/10.1073/pnas.2314096121 The structure of the Caenorhabditis elegans TMC-2 complex suggests roles of lipid-mediated subunit contacts in mechanosensory transduction

Sarah Clark ^{# 1}, Hanbin Jeong ^{# 1}, Rich Posert ¹, April Goehring ^{1 2}, Eric Gouaux ^{1 2 *}

¹Vollum Institute, Oregon Health and Science University, Portland, OR 97239.

²HHMI, Oregon Health and Science University, Portland, OR 97239.

^#These authors contributed equally
^*Corresponding author: correspondence to Eric Gouaux

Abstract

Mechanotransduction is the process by which a mechanical force, such as touch, is converted into an electrical signal. Transmembrane channel-like (TMC) proteins are an evolutionarily conserved family of membrane proteins whose function has been linked to a variety of mechanosensory processes, including hearing and balance sensation in vertebrates and locomotion in Drosophila. TMC1 and TMC2 are components of ion channel complexes, but the molecular features that tune these complexes to diverse mechanical stimuli are unknown. Caenorhabditis elegans express two TMC homologs, TMC-1 and TMC-2, both of which are the likely pore-forming subunits of mechanosensitive ion channels but differ in their expression pattern and functional role in the worm. Here, we present the single-particle cryo-electron microscopy structure of the native TMC-2 complex isolated from C. elegans. The complex is composed of two copies of the pore-forming TMC-2 subunit, the calcium and integrin binding protein CALM-1 and the transmembrane inner ear protein TMIE. Comparison of the TMC-2 complex to the recently published cryo-EM structure of the C. elegans TMC-1 complex highlights conserved protein-lipid interactions, as well as a π-helical structural motif in the pore-forming helices, that together suggest a mechanism for TMC-mediated mechanosensory transduction.

논문정보

형식Research article
게재일2024년 02월 (BRIC 등록일 2024-02-15)
연구진국외 연구진
분야 생명과학 > 구조생물 및 생물물리학

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