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TitleStructure and function of TM6SF1 reveals role in mTORC1 signaling.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 123, Issue 38, Page e2622424123, Year 2026
Publish dateSep 22, 2026
AuthorsSen Hong / Liangjie Jia / Rong Wang / Nadia Elghobashi-Meinhardt / Helen H Hobbs / Xiaochun Li /
PubMed AbstractThe transmembrane 6 superfamily (TM6SF) comprises two members: TM6SF1, a ubiquitously expressed lysosomal membrane protein of unknown function, and TM6SF2, an endoplasmic reticulum protein required ...The transmembrane 6 superfamily (TM6SF) comprises two members: TM6SF1, a ubiquitously expressed lysosomal membrane protein of unknown function, and TM6SF2, an endoplasmic reticulum protein required for bulk lipidation of Apolipoprotein B-containing lipoproteins. Here, we used cryo-electron microscopy (cryo-EM) to determine the structure of human TM6SF1 at 2.9-Å resolution. TM6SF1 forms a polytopic homodimer, with each protomer comprising 10 transmembrane helices (TMs). TMs 1-6 form a pocket that accommodates a cholesterol molecule. Cell-based assays revealed that loss of TM6SF1 perturbs mTORC1 signaling, resulting in reduced phosphorylation of S6 kinase 1 and 4E-BP1 and constitutive activation of transcription factor EB (TFEB), and that cholesterol is required for these effects. Biochemical analyses support the model that TM6SF1 directly engages LAMTOR1, a component of Ragulator complex, in a cholesterol-dependent manner. Together, these findings identify TM6SF1 as a lysosomal cholesterol binding protein involved in regulating mTORC1 signaling.
External linksProc Natl Acad Sci U S A / PubMed:42735304 / PubMed Central
MethodsEM (single particle)
Resolution2.86 - 3.37 Å
Structure data

75471

10up

EMDB-75471, PDB-10up:
Structure of human TM6SF1
Method: EM (single particle) / Resolution: 2.86 Å

75606

11br

EMDB-75606, PDB-11br:
Structure of cholesterol binding deficient human TM6SF1
Method: EM (single particle) / Resolution: 3.37 Å

Chemicals

ChemComp-CLR:
CHOLESTEROL

Source
  • Homo (humans)
  • homo sapiens (human)
KeywordsLIPID BINDING PROTEIN / Cholesterol / mTORC1 activity / Cholesterol binding protein

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