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TitleStructural insights into the LGR4-RSPO2-ZNRF3 complexes regulating WNT/β-catenin signaling.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 362, Year 2025
Publish dateJan 3, 2025
AuthorsLu Wang / Fangzheng Hu / Qianqian Cui / Huarui Qiao / Lingyun Li / Tengjie Geng / Yuying Li / Zengchao Sun / Siyu Zhou / Zhongyun Lan / Shaojue Guo / Ying Hu / Jiqiu Wang / Qilun Yang / Zenan Wang / Yuanyuan Dai / Yong Geng /
PubMed AbstractWNT/β-catenin signaling plays key roles in development and cancer. ZNRF3/RNF43 modulates Frizzleds through ubiquitination, dampening WNT/β-catenin signaling. Conversely, RSPO1-4 binding to LGR4-6 ...WNT/β-catenin signaling plays key roles in development and cancer. ZNRF3/RNF43 modulates Frizzleds through ubiquitination, dampening WNT/β-catenin signaling. Conversely, RSPO1-4 binding to LGR4-6 and ZNRF3/RNF43 enhances WNT/β-catenin signaling. Here, we elucidate the overall landscape of architectures in multiple LGR4, RSPO2, and ZNRF3 assemblies, showcasing varying stoichiometries and arrangements. These structures reveal that LGR4 and RSPO2 capture distinct states of ZNRF3. The intrinsic heterogeneity of the LGR4-RSPO2-ZNRF3 assembly is influenced by LGR4 content. Particularly, in the assembly complex with a 2:2:2 ratio, two LGR4 protomers induce and stabilize the inactive state of ZNRF3, characterized by a wide inward-open conformation of two transmembrane helices (TM helices). This specific assembly promotes a stable complex, facilitating LGR4-induced endocytosis of ZNRF3. In contrast, the active dimeric ZNRF3, bound by a single LGR4, adopts a coiled-coil TM helices conformation and dimerization of RING domains. Our findings unveil how LGR4 content mediates diverse assemblies, leading to conformational rearrangements in ZNRF3 to regulate WNT/β-catenin signaling, and provide a structural foundation for drug development targeting Wnt-driven cancers.
External linksNat Commun / PubMed:39753551 / PubMed Central
MethodsEM (single particle)
Resolution3.2 - 3.38 Å
Structure data

38307

8xfp

EMDB-38307, PDB-8xfp:
the pentamerA complex of LGR4-RSPO2-ZNRF3(delta RING)
Method: EM (single particle) / Resolution: 3.21 Å

38308

8xfs

EMDB-38308, PDB-8xfs:
LGR4-RSPO2-ZNRF3 RING domain (1:2:2)
Method: EM (single particle) / Resolution: 3.2 Å

38309

8xft

EMDB-38309, PDB-8xft:
LGR4-RSPO2-ZNRF3(1:1:1)
Method: EM (single particle) / Resolution: 3.24 Å

38982

8y69

EMDB-38982, PDB-8y69:
LGR4-RSPO2-ZNRF3 (2:2:2)
Method: EM (single particle) / Resolution: 3.38 Å

Chemicals

ChemComp-CLR:
CHOLESTEROL

Source
  • homo sapiens (human)
  • camelus bactrianus (Bactrian camel)
KeywordsMEMBRANE PROTEIN / LGR4-RSPO2-ZNRF3(delta RING) / lgr4 / znrf3 RING domain / 1:2:2 / ZNRF3 / 1:1:1 / RSPO2 / 2:2:2

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