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TitleTeneurin4 dimer structures reveal a calcium-stabilized compact conformation supporting homomeric trans-interactions.
Journal, issue, pagesEMBO J, Vol. 41, Issue 9, Page e107505, Year 2022
Publish dateMay 2, 2022
AuthorsDimphna H Meijer / Cátia P Frias / J Wouter Beugelink / Yanthi N Deurloo / Bert J C Janssen /
PubMed AbstractEstablishment of correct synaptic connections is a crucial step during neural circuitry formation. The Teneurin family of neuronal transmembrane proteins promotes cell-cell adhesion via homophilic ...Establishment of correct synaptic connections is a crucial step during neural circuitry formation. The Teneurin family of neuronal transmembrane proteins promotes cell-cell adhesion via homophilic and heterophilic interactions, and is required for synaptic partner matching in the visual and hippocampal systems in vertebrates. It remains unclear how individual Teneurins form macromolecular cis- and trans-synaptic protein complexes. Here, we present a 2.7 Å cryo-EM structure of the dimeric ectodomain of human Teneurin4. The structure reveals a compact conformation of the dimer, stabilized by interactions mediated by the C-rich, YD-shell, and ABD domains. A 1.5 Å crystal structure of the C-rich domain shows three conserved calcium binding sites, and thermal unfolding assays and SAXS-based rigid-body modeling demonstrate that the compactness and stability of Teneurin4 dimers are calcium-dependent. Teneurin4 dimers form a more extended conformation in conditions that lack calcium. Cellular assays reveal that the compact cis-dimer is compatible with homomeric trans-interactions. Together, these findings support a role for teneurins as a scaffold for macromolecular complex assembly and the establishment of cis- and trans-synaptic interactions to construct functional neuronal circuits.
External linksEMBO J / PubMed:35099835 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.4 - 3.7 Å
Structure data

EMDB-12122:
human Teneurin4 WT core
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-12123:
human Teneurin4 WT C1
Method: EM (single particle) / Resolution: 3.7 Å

12124

7bam

EMDB-12124, PDB-7bam:
human Teneurin4 WT C2
Method: EM (single particle) / Resolution: 3.5 Å

12125

7ban

EMDB-12125, PDB-7ban:
human Teneurin4 Mut C2
Method: EM (single particle) / Resolution: 2.7 Å

12126

7bao

EMDB-12126, PDB-7bao:
human Teneurin4 Mut C1
Method: EM (single particle) / Resolution: 2.7 Å

EMDB-12127:
human Teneurin4 Mut C-rich
Method: EM (single particle) / Resolution: 3.4 Å

PDB-7plp:
Human Teneurin-4 C-rich domain
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

Chemicals

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

ChemComp-CA:
Unknown entry

ChemComp-FE:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-NI:
NICKEL (II) ION

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / Synaptic cell adhesion / CELL ADHESION / cysteine-rich / calcium binding

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