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TitleThe structure of the TMC-2 complex suggests roles of lipid-mediated subunit contacts in mechanosensory transduction.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 121, Issue 8, Page e2314096121, Year 2024
Publish dateFeb 20, 2024
AuthorsSarah Clark / Hanbin Jeong / Rich Posert / April Goehring / Eric Gouaux /
PubMed AbstractMechanotransduction 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 ...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 . TMC1 and TMC2 are components of ion channel complexes, but the molecular features that tune these complexes to diverse mechanical stimuli are unknown. 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 . 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 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.
External linksProc Natl Acad Sci U S A / PubMed:38354260 / PubMed Central
MethodsEM (single particle)
Resolution2.9 Å
Structure data

41356

8tkp

EMDB-41356, PDB-8tkp:
Structure of the C. elegans TMC-2 complex
Method: EM (single particle) / Resolution: 2.9 Å

Chemicals

ChemComp-TWT:
DOCOSANE / Higher alkanes

ChemComp-PEE:
1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / DOPE, phospholipid*YM / Discrete optimized protein energy

ChemComp-R16:
HEXADECANE / Hexadecane

ChemComp-CLR:
CHOLESTEROL / Cholesterol

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-CA:
Unknown entry

ChemComp-PLM:
PALMITIC ACID / Palmitic acid

Source
  • caenorhabditis elegans (invertebrata)
KeywordsMEMBRANE PROTEIN / Mechanosensory transduction Macromolecular complex

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