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TitleCryo-EM Reveals Integrin-Mediated TGF-β Activation without Release from Latent TGF-β.
Journal, issue, pagesCell, Vol. 180, Issue 3, Page 490-501.e16, Year 2020
Publish dateFeb 6, 2020
AuthorsMelody G Campbell / Anthony Cormier / Saburo Ito / Robert I Seed / Andrew J Bondesson / Jianlong Lou / James D Marks / Jody L Baron / Yifan Cheng / Stephen L Nishimura /
PubMed AbstractIntegrin αvβ8 binds with exquisite specificity to latent transforming growth factor-β (L-TGF-β). This binding is essential for activating L-TGF-β presented by a variety of cell types. ...Integrin αvβ8 binds with exquisite specificity to latent transforming growth factor-β (L-TGF-β). This binding is essential for activating L-TGF-β presented by a variety of cell types. Inhibiting αvβ8-mediated TGF-β activation blocks immunosuppressive regulatory T cell differentiation, which is a potential therapeutic strategy in cancer. Using cryo-electron microscopy, structure-guided mutagenesis, and cell-based assays, we reveal the binding interactions between the entire αvβ8 ectodomain and its intact natural ligand, L-TGF-β, as well as two different inhibitory antibody fragments to understand the structural underpinnings of αvβ8 binding specificity and TGF-β activation. Our studies reveal a mechanism of TGF-β activation where mature TGF-β signals within the confines of L-TGF-β and the release and diffusion of TGF-β are not required. The structural details of this mechanism provide a rational basis for therapeutic strategies to inhibit αvβ8-mediated L-TGF-β activation.
External linksCell / PubMed:31955848 / PubMed Central
MethodsEM (single particle)
Resolution2.87 - 3.6 Å
Structure data

20794

6uja

EMDB-20794: Integrin alpha-v beta-8 in complex with latent TGF-beta (Primary map: sharpened. Additional map: unsharpened.)
PDB-6uja: Integrin alpha-v beta-8 in complex with pro-TGF-beta1
Method: EM (single particle) / Resolution: 3.3 Å

20795

6ujb

EMDB-20795: Integrin alpha-v beta-8 in complex with Fabs C6D4 and 11D12v2 (Primary map: sharpened, focused refinement. Five additional maps.)
PDB-6ujb: Integrin alpha-v beta-8 in complex with the Fabs C6D4 and 11D12v2
Method: EM (single particle) / Resolution: 3.51 Å

20796

6ujc

EMDB-20796: Integrin alpha-v beta-8 in complex with Fabs C6-RGD3 and 11D12v2 (Primary map: sharpened, focused refinement. Five additional maps.)
PDB-6ujc: Integrin alpha-v beta-8 in complex with the Fabs C6-RGD3 and 11D12v2
Method: EM (single particle) / Resolution: 3.56 Å

EMDB-20797:
Integrin alpha-v beta-8 in complex with latent TGF-beta, Conformation i (Primary map: sharpened. Additional map: unsharpened.)
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-20798:
Integrin alpha-v beta-8 in complex with latent TGF-beta, Conformation ii (Primary map: sharpened. Additional map: unsharpened.)
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-20799:
Integrin alpha-v beta-8 in complex with latent TGF-beta, Conformation iii (Primary map: sharpened. Additional map: unsharpened.)
Method: EM (single particle) / Resolution: 3.57 Å

EMDB-20800:
Integrin alpha-v beta-8 in complex with latent TGF-beta, Conformation v (Primary map: sharpened. Additional map: unsharpened.)
Method: EM (single particle) / Resolution: 3.48 Å

EMDB-20801:
Integrin alpha-v beta-8 in complex with latent TGF-beta, Conformation vi (Primary map: sharpened. Additional map: unsharpened.)
Method: EM (single particle) / Resolution: 3.51 Å

EMDB-20802:
Integrin alpha-v beta-8 in complex with latent TGF-beta, Conformation vii (Primary map: sharpened. Additional map: unsharpened.)
Method: EM (single particle) / Resolution: 3.45 Å

EMDB-21125:
Integrin alpha-v beta-8 in complex with pro-TGF-beta1
Method: EM (single particle) / Resolution: 2.87 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
  • sus scrofa (pig)
  • mus musculus (house mouse)
KeywordsSIGNALING PROTEIN / glycoprotein / adhesion / signaling / SIGNALING PROTEIN/IMMUNE SYSTEM / SIGNALING PROTEIN-IMMUNE SYSTEM complex

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