Journal
STRUCTURE
Volume 27, Issue 6, Pages 893-+Publisher
CELL PRESS
DOI: 10.1016/j.str.2019.03.004
Keywords
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Funding
- RWJ Foundation [74260]
- NJDOH [CBIR16PIL035]
- National Science Foundation [IOS-1755189, MCB-1450895, DMR-1332208]
- NIH [R01 NS097161, GM120600]
- NSF [NSF-ACI-1339649]
- NSF/XSEDE grant [TG-MCB070039N]
- UT grant [TG457201]
- NIGMS [T32 GM008339]
- National Institute of General Medical Sciences, NIH [GM-103485]
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In the developing brain, cell-surface proteins play crucial roles, but their protein-protein interaction network remains largely unknown. A proteomic screen identified 200 interactions, 89 of which were not previously published. Among these interactions, we find that the IgLONs, a family of five cell-surface neuronal proteins implicated in various human disorders, interact as homo- and heterodimers. We reveal their interaction patterns and report the dimeric crystal structures of Neurotrimin (NTRI), IgLON5, and the neuronal growth regulator 1 (NEGR1)/IgLON5 complex. We show that IgLONs maintain an extended conformation and that their dimerization occurs through the first Ig domain of each monomer and is Ca2+ independent. Cell aggregation shows that NTRI and NEGR1 homo-and heterodimerize in trans. Taken together, we report 89 unpublished cell-surface ligand-receptor pairs and describe structural models of trans interactions of IgLONs, showing that their structures are compatible with a model of interaction across the synaptic cleft.
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