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TitleMolecular basis of TMED9 oligomerization and entrapment of misfolded protein cargo in the early secretory pathway.
Journal, issue, pagesSci Adv, Vol. 10, Issue 38, Page eadp2221, Year 2024
Publish dateSep 20, 2024
AuthorsLe Xiao / Xiong Pi / Alissa C Goss / Tarick El-Baba / Julian F Ehrmann / Elizabeth Grinkevich / Silvana Bazua-Valenti / Valeria Padovano / Seth L Alper / Dominique Carey / Namrata D Udeshi / Steven A Carr / Juan Lorenzo Pablo / Carol V Robinson / Anna Greka / Hao Wu /
PubMed AbstractIntracellular accumulation of misfolded proteins causes serious human proteinopathies. The transmembrane emp24 domain 9 (TMED9) cargo receptor promotes a general mechanism of cytotoxicity by ...Intracellular accumulation of misfolded proteins causes serious human proteinopathies. The transmembrane emp24 domain 9 (TMED9) cargo receptor promotes a general mechanism of cytotoxicity by entrapping misfolded protein cargos in the early secretory pathway. However, the molecular basis for this TMED9-mediated cargo retention remains elusive. Here, we report cryo-electron microscopy structures of TMED9, which reveal its unexpected self-oligomerization into octamers, dodecamers, and, by extension, even higher-order oligomers. The TMED9 oligomerization is driven by an intrinsic symmetry mismatch between the trimeric coiled coil domain and the tetrameric transmembrane domain. Using frameshifted Mucin 1 as an example of aggregated disease-related protein cargo, we implicate a mode of direct interaction with the TMED9 luminal Golgi-dynamics domain. The structures suggest and we confirm that TMED9 oligomerization favors the recruitment of coat protein I (COPI), but not COPII coatomers, facilitating retrograde transport and explaining the observed cargo entrapment. Our work thus reveals a molecular basis for TMED9-mediated misfolded protein retention in the early secretory pathway.
External linksSci Adv / PubMed:39303030 / PubMed Central
MethodsEM (single particle)
Resolution3.7 - 5.5 Å
Structure data

45634

9cjk

EMDB-45634, PDB-9cjk:
Human TMED9 octamer structure
Method: EM (single particle) / Resolution: 3.7 Å

45635

9cjl

EMDB-45635, PDB-9cjl:
Molecular basis of TMED9 dodecamer
Method: EM (single particle) / Resolution: 5.5 Å

Chemicals


ChemComp, No image

ChemComp-9ED:
Unknown entry

Source
  • homo sapiens (human)
KeywordsPROTEIN TRANSPORT / tmed9 / misfolded protein / secretory pathway / Cryo-EM

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