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Carbonic anhydrase-...
Carbonic anhydrase-related protein CA10 is an evolutionarily conserved pan-neurexin ligand
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Sterky, F. H. (författare)
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Trotter, J. H. (författare)
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Lee, S. J. (författare)
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- Recktenwald, Christian V (författare)
- Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för medicinsk kemi och cellbiologi,Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
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Du, X. (författare)
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Zhou, B. (författare)
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Zhou, P. (författare)
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Schwenk, J. (författare)
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Fakler, B. (författare)
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Sudhof, T. C. (författare)
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(creator_code:org_t)
- 2017-02
- 2017
- Engelska.
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Ingår i: Proceedings of the National Academy of Sciences of the United States of America. - : Proceedings of the National Academy of Sciences. - 0027-8424. ; 114:7
- Relaterad länk:
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https://www.pnas.org...
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https://gup.ub.gu.se...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinsk bioteknologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Medical Biotechnology (hsv//eng)
Nyckelord
- Car10
- Car11
- synapse
- cell adhesion
- cell-surface proteins
- synapse formation
- beta-neurexins
- tyrosine
- phosphatases
- receptor
- alpha
- domain
- brain
- gene
- viii
- Science & Technology - Other Topics
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
Hitta via bibliotek
Till lärosätets databas
- Av författaren/redakt...
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Sterky, F. H.
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Trotter, J. H.
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Lee, S. J.
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Recktenwald, Chr ...
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Du, X.
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Zhou, B.
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visa fler...
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Zhou, P.
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Schwenk, J.
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Fakler, B.
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Sudhof, T. C.
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visa färre...
- Om ämnet
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- MEDICIN OCH HÄLSOVETENSKAP
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MEDICIN OCH HÄLS ...
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och Medicinsk biotek ...
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Proceedings of t ...
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Proceedings of t ...
- Av lärosätet
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Göteborgs universitet