A proteomic screen of neuronal cell-surface molecules reveals IgLONs as structurally conserved interaction modules at the synapse

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dc.contributor.authorRanaivoson, Fanomezana M.
dc.contributor.authorTurk, Liam S.
dc.contributor.authorOzgul, Sinem
dc.contributor.authorKakehi, Sumie
dc.contributor.authorvon Daake, Sventja
dc.contributor.authorLopez, Nicole
dc.contributor.authorTrobiani, Laura
dc.contributor.authorDe Jaco, Antonella
dc.contributor.authorDenissova, Natalia
dc.contributor.authorDemeler, Borries
dc.contributor.authorÖzkan, Engin
dc.contributor.authorMontelione, Gaetano T.
dc.contributor.authorComoletti, Davide
dc.date.accessioned2021-08-23T17:32:57Z
dc.date.available2021-08-23T17:32:57Z
dc.date.issued2019
dc.descriptionAccepted author manuscripten_US
dc.description.abstractIn 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 Taken together, we report 89 unpublished cell-surface ligand-receptor pairs and describe structural models of trans interactions of IgLONs, showing that their structures are compatible with a model of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.en_US
dc.description.peer-reviewYesen_US
dc.identifier.citationRanaivoson, F. M., Turk, L. S., Ozgul, S., Kakehi, S., von Daake, S., Lopez, N., Trobiani, L., De Jaco, A., Denissova, N., Demeler, B., Özcan, E., Montelione, G. T., & Comoletti, D. (2019). A proteomic screen of neuronal cell-surface molecules reveals IgLONs as structurally conserved interaction molecules at the synapse. Structure, 27(6), 893-906. https://doi.org/10.1016/j.str.2019.03.004en_US
dc.identifier.urihttps://hdl.handle.net/10133/6009
dc.language.isoen_USen_US
dc.publisherCell Pressen_US
dc.publisher.departmentDepartment of Chemistry and Biochemistryen_US
dc.publisher.facultyArts and Scienceen_US
dc.publisher.institutionChild Health Institute of New Jerseyen_US
dc.publisher.institutionSapienza University of Romeen_US
dc.publisher.institutionRutgers Universityen_US
dc.publisher.institutionUniversity of Lethbridgeen_US
dc.publisher.institutionUniversity of Chicagoen_US
dc.publisher.urlhttps://doi.org/10.1016/j.str.2019.03.004en_US
dc.subjectLigand-receptor pairen_US
dc.subjectELISAen_US
dc.subjectIgLONen_US
dc.subjectProtein crystallographyen_US
dc.subjectSAXSen_US
dc.subjectCell-surface
dc.subject.lcshEnzyme-linked immunosorbent assay
dc.titleA proteomic screen of neuronal cell-surface molecules reveals IgLONs as structurally conserved interaction modules at the synapseen_US
dc.typeArticleen_US
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