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TitleStructural basis for regulation of CELSR1 by a compact module in its extracellular region.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 3972, Year 2025
Publish dateApr 28, 2025
AuthorsSumit J Bandekar / Krassimira Garbett / Szymon P Kordon / Ethan E Dintzner / Jingxian Li / Tanner Shearer / Richard C Sando / Demet Araç /
PubMed AbstractThe Cadherin EGF Laminin G seven-pass G-type receptor subfamily (CELSR/ADGRC) is one of the most conserved among adhesion G protein-coupled receptors and is essential for animal development. The ...The Cadherin EGF Laminin G seven-pass G-type receptor subfamily (CELSR/ADGRC) is one of the most conserved among adhesion G protein-coupled receptors and is essential for animal development. The extracellular regions (ECRs) of CELSRs are large with 23 adhesion domains. However, molecular insight into CELSR function is sparsely available. Here, we report the 3.8 Å cryo-EM reconstruction of the mouse CELSR1 ECR and reveal that 14 domains form a compact module mediated by conserved interactions majorly between the CADH9 and C-terminal GAIN domains. In the presence of Ca, the CELSR1 ECR forms a dimer species mediated by the cadherin repeats putatively in an antiparallel fashion. Cell-based assays reveal the N-terminal CADH1-8 repeat is required for cell-cell adhesion and the C-terminal CADH9-GAIN compact module can regulate cellular adhesion. Our work provides molecular insight into how one of the largest GPCRs uses defined structural modules to regulate receptor function.
External linksNat Commun / PubMed:40295529 / PubMed Central
MethodsEM (single particle)
Resolution4.3 Å
Structure data

43644

8vy2

EMDB-43644, PDB-8vy2:
Structure of mCELSR1 extracellular region containing CADH9-GAIN domains
Method: EM (single particle) / Resolution: 4.3 Å

Chemicals

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

Source
  • mus musculus (house mouse)
KeywordsSIGNALING PROTEIN / CELSR / adhesion / GPCR / planar cell polarity

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