8r51

Mouse teneurin-3 non-compact subunit - A1B1 isoform

spinqualitylabelsall models 8r51, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8r51 is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.2Å Ligands: NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TEN3_MOUSE Involved in neural development by regulating the establishment of proper connectivity within the nervous system (PubMed:17478416, PubMed:17803360, PubMed:23028443, PubMed:25406022, PubMed:22499796, PubMed:29414938). Acts in both pre- and postsynaptic neurons in the hippocampus to control the assembly of a precise topographic projection: required in both CA1 and subicular neurons for the precise targeting of proximal CA1 axons to distal subiculum, probably by promoting homophilic cell adhesion (PubMed:29414938). Promotes homophilic adhesion in a splicing isoform-dependent manner: most isoforms (isoform-type A and type-B) can mediate homophilic interaction (PubMed:29414938). Promotes axon guidance (PubMed:23028443). Required for proper dendrite morphogenesis and axon targeting in the vertebrate visual system, thereby playing a key role in the development of the visual pathway (PubMed:17803360, PubMed:23028443, PubMed:25406022, PubMed:22499796). Regulates the formation in ipsilateral retinal mapping to both the dorsal lateral geniculate nucleus (dLGN) and the superior colliculus (SC) (PubMed:17803360, PubMed:23028443). May also be involved in the differentiation of the fibroblast-like cells in the superficial layer of mandibular condylar cartilage into chondrocytes (PubMed:20636325). Publication Abstract from PubMed Neuronal network formation is facilitated by recognition between synaptic cell adhesion molecules at the cell surface. Alternative splicing of cell adhesion molecules provides additional specificity in forming neuronal connections. For the teneurin family of cell adhesion molecules, alternative splicing of the EGF-repeats and NHL domain controls synaptic protein-protein interactions. Here we present cryo-EM structures of the compact dimeric ectodomain of two teneurin-3 isoforms that harbour the splice insert in the EGF-repeats. This dimer is stabilised by an EGF8-ABD contact between subunits. Cryo-EM reconstructions of all four splice variants, together with SAXS and negative stain EM, reveal compacted dimers for each, with variant-specific dimeric arrangements. This results in specific trans-cellular interactions, as tested in cell clustering and stripe assays. The compact conformations provide a structural basis for teneurin homo- and heterophilic interactions. Altogether, our findings demonstrate how alternative splicing results in rearrangements of the dimeric subunits, influencing neuronal recognition and likely circuit wiring. Alternative splicing controls teneurin-3 compact dimer formation for neuronal recognition.,Gogou C, Beugelink JW, Frias CP, Kresik L, Jaroszynska N, Drescher U, Janssen BJC, Hindges R, Meijer DH Nat Commun. 2024 Apr 29;15(1):3648. doi: 10.1038/s41467-024-47763-x. PMID:38684645 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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