RGD Reference Report - Characterization of the interaction of a recombinant soluble neuroligin-1 with neurexin-1beta. - Rat Genome Database

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Characterization of the interaction of a recombinant soluble neuroligin-1 with neurexin-1beta.

Authors: Comoletti, Davide  Flynn, Robyn  Jennings, Lori L  Chubykin, Alexander  Matsumura, Takehito  Hasegawa, Hana  Südhof, Thomas C  Taylor, Palmer 
Citation: Comoletti D, etal., J Biol Chem. 2003 Dec 12;278(50):50497-505. Epub 2003 Sep 30.
RGD ID: 13210536
Pubmed: PMID:14522992   (View Abstract at PubMed)
DOI: DOI:10.1074/jbc.M306803200   (Journal Full-text)

Neuroligins, proteins of the alpha/beta-hydrolase fold family, are found as postsynaptic transmembrane proteins whose extracellular domain associates with presynaptic partners, proteins of the neurexin family. To characterize the molecular basis of neuroligin interaction with neurexin-beta, we expressed five soluble and exportable forms of neuroligin-1 from recombinant DNA sources, by truncating the protein before the transmembrane span near its carboxyl terminus. The extracellular domain of functional neuroligin-1 associates as a dimer when analyzed by sedimentation equilibrium. By surface plasmon resonance, we established that soluble neuroligins-1 bind neurexin-1beta, but the homologous alpha/beta-hydrolase fold protein, acetylcholinesterase, failed to associate with the neurexins. Neuroligin-1 has a unique N-linked glycosylation pattern in the neuroligin family, and glycosylation and its processing modify neuroligin activity. Incomplete processing of the protein and enzymatic removal of the oligosaccharides chain or the terminal sialic acids from neuroligin-1 enhance its activity, whereas deglycosylation of neurexin-1beta did not alter its association capacity. In particular, the N-linked glycosylation at position 303 appears to be a major determinant in modifying the association with neurexin-1beta. We show here that glycosylation processing of neuroligin, in addition to mRNA splicing and gene selection, contributes to the specificity of the neurexin-beta/neuroligin-1 association.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Nlgn1Ratcellular response to calcium ion involved_inIDA PMID:14522992ARUK-UCL 
Nrxn1Ratcellular response to calcium ion involved_inIDA PMID:14522992ARUK-UCL 

Cellular Component

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Nlgn1Ratprotein complex involved in cell-cell adhesion part_ofIPI PMID:14522992ComplexPortal 
Nrxn1Ratprotein complex involved in cell-cell adhesion part_ofIPI PMID:14522992ComplexPortal 

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Nlgn1Ratneurexin family protein binding enablesIPIUniProtKB:Q63373PMID:14522992ARUK-UCL 
Nrxn1Ratneuroligin family protein binding enablesIPIUniProtKB:Q62765PMID:14522992ARUK-UCL 

Objects Annotated

Genes (Rattus norvegicus)
Nlgn1  (neuroligin 1)
Nrxn1  (neurexin 1)


Additional Information