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TitleThree cryo-EM structures of CD109 reveal its mechanism of protease inhibition.
Journal, issue, pagesCell Rep, Vol. 44, Issue 6, Page 115787, Year 2025
Publish dateJun 24, 2025
AuthorsAna V Almeida / Kathrine T Jensen / Seandean L Harwood / Martin H Jørgensen / Nadia S Nielsen / Ida B Thøgersen / Jan J Enghild / Gregers R Andersen /
PubMed AbstractCD109 is a glycosylphosphatidylinositol-anchored protein. In addition to regulating transforming growth factor β (TGF-β) network signaling, CD109 is also a protease inhibitor. Protease cleavage of ...CD109 is a glycosylphosphatidylinositol-anchored protein. In addition to regulating transforming growth factor β (TGF-β) network signaling, CD109 is also a protease inhibitor. Protease cleavage of its bait region triggers a conformational change releasing the major fragment from the cell surface, exposing a reactive thioester that can conjugate proteases. To understand this protease inhibition mechanism, we determined cryoelectron microscopy structures of CD109 in native, protease-activated, and methylamine-activated conformations. Despite CD109's low sequence similarity with the protease inhibitor A2ML1, CD109 adopts a similar protease-activated conformation, suggesting a shared mechanism of protease inhibition. Deglycosylation of CD109 does not affect chymotrypsin conjugation but enhances substrate access, suggesting that CD109 glycans contribute to protease inhibition. Our data provide a structural basis for understanding CD109's protease-triggered membrane release, its protease inhibitory mechanism, and additional biological functions.
External linksCell Rep / PubMed:40482031
MethodsEM (single particle)
Resolution2.99 - 3.3 Å
Structure data

19699

8s3o

EMDB-19699, PDB-8s3o:
Structure of native human CD109
Method: EM (single particle) / Resolution: 2.99 Å

50841

9fx2

EMDB-50841, PDB-9fx2:
Structure of methylamine activated CD109
Method: EM (single particle) / Resolution: 3.3 Å

50842

9fx3

EMDB-50842, PDB-9fx3:
Structure of active human CD109
Method: EM (single particle) / Resolution: 3.2 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • homo sapiens (human)
KeywordsIMMUNE SYSTEM / Protease inhibitor / Native conformation / Alfa-macroglobulin / thioester activation / intermediate conformation / alpha-macroglobulin / Protease cleaved / Active conformation

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