Structural basis of cooling agent and lipid sensing by the cold-activated TRPM8 channel | Zendy

Ying Yin | Zendy; Son C. Le | Zendy; Allen L. Hsu | Zendy; Mario J. Borgnia | Zendy; Huanghe Yang | Zendy; SeokYong Lee | Zendy

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Structural basis of cooling agent and lipid sensing by the cold-activated TRPM8 channel

Author(s) -

Ying Yin,

Son C. Le,

Allen L. Hsu,

Mario J. Borgnia,

Huanghe Yang,

SeokYong Lee

Publication year - 2019

Publication title -

science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 12.556

H-Index - 1186

eISSN - 1095-9203

pISSN - 0036-8075

DOI - 10.1126/science.aav9334

Subject(s) - trpm8 , transient receptor potential channel , allosteric regulation , chemistry , menthol , phosphatidylinositol , biophysics , biochemistry , receptor , signal transduction , biology , organic chemistry , trpv1

Cool mechanism for sensing cool In humans, cold is primarily sensed by transient receptor potential melastatin member 8 (TRPM8), a calcium channel. Yinet al. present cryo–electron microscopy structures of TRPM8 with cooling agents, membrane lipid phosphatidylinositol-4,5-bisphosphate (PIP2), and calcium. Structural and functional analyses showed that the PIP2 binding site in TRPM8 is completely different from PIP2 sites in other TRP channels. The binding of PIP2 and cooling agents allosterically enhance each other and activate the channel opening. Thus, the activation mechanism of TRPM8 is distinct from that used by other TRP channels.Science , this issue p.eaav9334

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