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Carbonic anhydrase-related protein CA10 is an evolutionarily conserved pan-neurexin ligand

Artikel i vetenskaplig tidskrift
Författare F. H. Sterky
J. H. Trotter
S. J. Lee
Christian V Recktenwald
X. Du
B. Zhou
P. Zhou
J. Schwenk
B. Fakler
T. C. Sudhof
Publicerad i Proceedings of the National Academy of Sciences of the United States of America
Volym 114
Nummer/häfte 7
Sidor E1253-E1262
ISSN 0027-8424
Publiceringsår 2017
Publicerad vid Institutionen för biomedicin, avdelningen för medicinsk kemi och cellbiologi
Sidor E1253-E1262
Språk en
Länkar dx.doi.org/10.1073/pnas.1621321114
Ämnesord Car10, Car11, synapse, cell adhesion, cell-surface proteins, synapse formation, beta-neurexins, tyrosine, phosphatases, receptor, alpha, domain, brain, gene, viii, Science & Technology - Other Topics
Ämneskategorier Medicinsk bioteknologi

Sammanfattning

Establishment, specification, and validation of synaptic connections are thought to be mediated by interactions between pre- and postsynaptic cell-adhesion molecules. Arguably, the best-characterized transsynaptic interactions are formed by presynaptic neurexins, which bind to diverse postsynaptic ligands. In a proteomic screen of neurexin-1 (Nrxn1) complexes immunoisolated from mouse brain, we identified carbonic anhydrase-related proteins CA10 and CA11, two homologous, secreted glycoproteins of unknown function that are predominantly expressed in brain. We found that CA10 directly binds in a cis configuration to a conserved membrane-proximal, extracellular sequence of alpha- and beta-neurexins. The CA10neurexin complex is stable and stoichiometric, and results in formation of intermolecular disulfide bonds between conserved cysteine residues in neurexins and CA10. CA10 promotes surface expression of alpha- and beta-neurexins, suggesting that CA10 may form a complex with neurexins in the secretory pathway that facilitates surface transport of neurexins. Moreover, we observed that the Nrxn1 gene expresses from an internal 3' promoter a third isoform, Nrxn1 gamma, that lacks all Nrxn1 extracellular domains except for the membrane-proximal sequences and that also tightly binds to CA10. Our data expand the understanding of neurexin-based transsynaptic interaction networks by providing further insight into the interactions nucleated by neurexins at the synapse.

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