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TitleStructures of TGF-β with betaglycan and signaling receptors reveal mechanisms of complex assembly and signaling.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 1778, Year 2025
Publish dateFeb 26, 2025
AuthorsŁukasz Wieteska / Alexander B Taylor / Emma Punch / Jonathan A Coleman / Isabella O Conway / Yeu-Farn Lin / Chang-Hyeock Byeon / Cynthia S Hinck / Troy Krzysiak / Rieko Ishima / Fernando López-Casillas / Peter Cherepanov / Daniel J Bernard / Caroline S Hill / Andrew P Hinck /
PubMed AbstractBetaglycan (BG) is a transmembrane co-receptor of the transforming growth factor-β (TGF-β) family of signaling ligands. It is essential for embryonic development, tissue homeostasis and fertility ...Betaglycan (BG) is a transmembrane co-receptor of the transforming growth factor-β (TGF-β) family of signaling ligands. It is essential for embryonic development, tissue homeostasis and fertility in adults. It functions by enabling binding of the three TGF-β isoforms to their signaling receptors and is additionally required for inhibin A (InhA) activity. Despite its requirement for the functions of TGF-βs and InhA in vivo, structural information explaining BG ligand selectivity and its mechanism of action is lacking. Here, we determine the structure of TGF-β bound both to BG and the signaling receptors, TGFBR1 and TGFBR2. We identify key regions responsible for ligand engagement, which has revealed binding interfaces that differ from those described for the closely related co-receptor of the TGF-β family, endoglin, thus demonstrating remarkable evolutionary adaptation to enable ligand selectivity. Finally, we provide a structural explanation for the hand-off mechanism underlying TGF-β signal potentiation.
External linksNat Commun / PubMed:40011426 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution3 - 6.39 Å
Structure data

EMDB-50326: Betaglycan in complex with TGF-b1
Method: EM (single particle) / Resolution: 6.39 Å

50333

9fdy

EMDB-50333, PDB-9fdy:
Betaglycan Orphan Domain (ratBGo) in complex with TGF-b1 and extracellular domain of TGFBRII
Method: EM (single particle) / Resolution: 3.4 Å

50519

9fk5

EMDB-50519, PDB-9fk5:
Zebrafish Betaglycan Orphan Domain (zfBGo) in complex with TGF-B3 and extracellular domains of TGFBRI and TGFBRII
Method: EM (single particle) / Resolution: 4.1 Å

50524

9fkp

EMDB-50524, PDB-9fkp:
Zebrafish Betaglycan Orphan Domain (zfBGo) in complex with TGF-b1 and extracellular domain of TGFBRII
Method: EM (single particle) / Resolution: 3.72 Å

PDB-9b9f:
Zebrafish Betaglycan Orphan Domain (zfBGo) in complex with TGF-B3 and extracellular domains of TGFBRI and TGFBRII
Method: X-RAY DIFFRACTION / Resolution: 3 Å

Source
  • rattus norvegicus (Norway rat)
  • homo sapiens (human)
  • danio rerio (zebrafish)
KeywordsMEMBRANE PROTEIN / Complex / Betaglycan / TGFBR3 / TGFb / TGFBR1 / TGFBR2 / TGFb1

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