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TitleCryo-EM structure of mouse TRPML2 in lipid nanodiscs.
Journal, issue, pagesJ Biol Chem, Vol. 298, Issue 2, Page 101487, Year 2022
Publish dateDec 14, 2021
AuthorsXiaojing Song / Jian Li / Miao Tian / Huaiyi Zhu / Xiaohui Hu / Yuting Zhang / Yanru Cao / Heyang Ye / Peter J McCormick / Bo Zeng / Yang Fu / Jingjing Duan / Jin Zhang /
PubMed AbstractIn mammalians, transient receptor potential mucolipin ion channels (TRPMLs) exhibit variable permeability to cations such as Ca, Fe, Zn, and Na and can be activated by the phosphoinositide PI(3,5)P2 ...In mammalians, transient receptor potential mucolipin ion channels (TRPMLs) exhibit variable permeability to cations such as Ca, Fe, Zn, and Na and can be activated by the phosphoinositide PI(3,5)P2 in the endolysosomal system. Loss or dysfunction of TRPMLs has been implicated in lysosomal storage disorders, infectious diseases, and metabolic diseases. TRPML2 has recently been identified as a mechanosensitive and hypotonicity-sensitive channel in endolysosomal organelles, which distinguishes it from TRPML1 and TRPML3. However, the molecular and gating mechanism of TRPML2 remains elusive. Here, we present the cryo-EM structure of the full-length mouse TRPML2 in lipid nanodiscs at 3.14 Å resolution. The TRPML2 homotetramer structure at pH 7.4 in the apo state reveals an inactive conformation and some unique features of the extracytosolic/luminal domain and voltage sensor-like domain that have implications for the ion-conducting pathway. This structure enables new comparisons between the different subgroups of TRPML channels with available structures and provides structural insights into the conservation and diversity of TRPML channels. These comparisons have broad implications for understanding a variety of molecular mechanisms of TRPMLs in different pH conditions, including with and without bound agonists and antagonists.
External linksJ Biol Chem / PubMed:34915027 / PubMed Central
MethodsEM (single particle)
Resolution3.18 Å
Structure data

30924

7dys

EMDB-30924, PDB-7dys:
CryoEM structure of full length mouse TRPML2
Method: EM (single particle) / Resolution: 3.18 Å

Source
  • mus musculus (house mouse)
KeywordsMEMBRANE PROTEIN / transient receptor potential mucolipin channels / TRP channel / TRPML2

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