Neurexins

Geppert, M.; Ushkaryov, Yuri A.; Hata, Y.; Davletov, Bazbek; Petrenko, Alexander G.; Südhof, Thomas C.

doi:10.1101/sqb.1992.057.01.053

Cited by 21 publications

(7 citation statements)

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“…Neurexins represent a family of polymorphic cell surface proteins with receptor-like structures (1)(2)(3)(4). We have proposed that neurexins might function as cell recognition molecules in mediating cell/cell interactions in the nervous system.…”

Section: Discussionmentioning

confidence: 99%

“…Cell recognition processes between neurons are likely to contribute to the establishment and maintenance of this network, but little is known about the mechanisms involved. Neurexins constitute a family of polymorphic cell surface proteins that are candidates for mediating cell recognition between neurons (1,2). Three mammalian genes for neurexins are known.…”

Section: ؉mentioning

confidence: 99%

“…Three mammalian genes for neurexins are known. Each gene has two promoters that drive the synthesis of long and short classes of transcripts (1)(2)(3)(4). The long transcripts encode ␣-neurexins, and the short transcripts encode ␤-neurexins.…”

Section: ؉mentioning

confidence: 99%

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Binding Properties of Neuroligin 1 and Neurexin 1β Reveal Function as Heterophilic Cell Adhesion Molecules

Nguyen

Südhof

1997

Journal of Biological Chemistry

216

170

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␤-Neurexins and neuroligins are plasma membrane proteins that are displayed on the neuronal cell surface. We have now investigated the interaction of neurexin 1␤ with neuroligin 1 to evaluate their potential to function as heterophilic cell adhesion molecules. Using detergent-solubilized neuroligins and secreted neurexin 1␤-IgG fusion protein, we observed binding of these proteins to each other only in the presence of Ca 2؉ and in no other divalent cation tested. Only neurexin 1␤ lacking an insert in splice site 4 bound neuroligins, whereas neurexin 1␤ containing an insert was inactive. Halfmaximal binding required 1-3 M free Ca 2؉, which probably acts by binding to neuroligin 1 but not to neurexin 1␤. To determine if neurexin 1␤ and neuroligin 1 can also interact with each other when present in a native membrane environment on the cell surface, we generated transfected cell lines expressing neuroligin 1 and neurexin 1␤. Upon mixing different cell populations, we found that cells aggregate only if cells expressing neurexin 1␤ are mixed with cells expressing neuroligin 1. Aggregation was dependent on Ca 2؉ and was inhibited by the addition of soluble neurexin 1␤ lacking an insert in splice site 4 but not by the addition of neurexin 1␤ containing an insert in splice site 4. We conclude that neurexin 1␤ and neuroligin 1 (and, by extension, other ␤-neurexins and neuroligins) function as heterophilic cell adhesion molecules in a Ca 2؉ -dependent reaction that is regulated by alternative splicing of ␤-neurexins.Neurons in the brain are connected to each other by thousands of synapses, creating a dense network of communicating cells. Cell recognition processes between neurons are likely to contribute to the establishment and maintenance of this network, but little is known about the mechanisms involved. Neurexins constitute a family of polymorphic cell surface proteins that are candidates for mediating cell recognition between neurons (1, 2). Three mammalian genes for neurexins are known. Each gene has two promoters that drive the synthesis of long and short classes of transcripts (1-4). The long transcripts encode ␣-neurexins, and the short transcripts encode ␤-neurexins. Both transcripts are detectable only in neurons (1, 5).␣-and ␤-neurexins are type I membrane proteins that resemble cell surface receptors and are composed of canonical sets of domains. The extracellular sequences of ␣-neurexins contain a classical N-terminal signal peptide followed by six weakly homologous repeats with interspersed EGF 1 -like sequences. The six repeats are related to repeated sequences found in a number of proteins and were first described in the G domain of laminin A, sex hormone-binding globulin, and neurexins (1, 6, 7). For this reason we call these repeats LNS (laminin/neurexin/sex hormone-binding globulin) domains. In ␣-neurexins, EGF-like sequences are placed after the first, third, and fifth LNS domain. After the sixth LNS domain, ␣-neurexins contain a short serine/threonine-rich sequence that is probably O-glycosylated (4)....

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Section: Discussionmentioning

confidence: 99%

Section: ؉mentioning

confidence: 99%

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Binding Properties of Neuroligin 1 and Neurexin 1β Reveal Function as Heterophilic Cell Adhesion Molecules

Nguyen

Südhof

1997

Journal of Biological Chemistry

216

170

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“…Neurexin mRNAs were only found in brain-related tissues [42], which perfectly correlates with the distribution of the a-latrotoxin receptor [7]. At least three different neurexins exist [29]. Each of these have two forms (a, the longer; and /?, the shorter, sharing the same C-terminal region), which are probably the results of transcription from alternative promoters.…”

Section: Identification and Molecular Clon-ing Of The A-latrotoxin Rementioning

confidence: 99%

α‐Latrotoxin receptor

Petrenko

1993

FEBS Letters

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a-Latrotoxin is a potent stimulator of neurotransmitter release from nerve terminals. High affinity membrane cl-latrotoxin receptor was purified in an active binding form. It is a membrane glycoprotein (M, 160,00~220,000) which may be complexed to a smaller polypeptide (M, 29,000). The structure of the receptor protein suggests that it may be a synapse-specific cell recognition molecule. Intracellularly, the tx-latrotoxin receptor interacts with synaptotagmin, a calcium-and phospholipid-binding protein specifically localized in the synaptic vesicle membrane. This interaction may be important for targeting of synaptic vesicles to presynaptic release sites.

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“…a-latroinsectotoxin has demonstrated a similar structural organisation of the neurotoxins (Kiyatkin et al, 1990(Kiyatkin et al, , 1993). An 81-kDa central domain comprised of 20 ankyrin-like repeats has been proposed as a likely candidate for the translocated domain (Geppert et al, 1992). However, it has been shown that a-latrotoxin and a-latroinsectotoxin usually co-purify with an 8-kDA low-molecular-mass protein which is an abundant component of black widow spider venom (Kiyatkin et al, 1992).…”

mentioning

confidence: 99%

Functional Characterization of Black Widow Spider Neurotoxins Synthesised in Insect Cells

Kiyatkin

Kulikovskaya

Grishin

et al. 1995

European Journal of Biochemistry

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α‐latrotoxin, α‐latroinsectotoxin and the low‐molecular‐mass protein from black widow spider venom were synthesised in insect cells using the baculovirus expression system. SDS/PAGE analysis of recombinant‐virus‐infected cells revealed novel proteins that migrated with sizes similar to those of the neurotoxins from spider venom. The identities of these proteins as α‐latrotoxin, α‐latroinsectotoxin or the low‐molecular‐mass protein were confirmed by immunoblot analysis of infected cells with anti‐(α‐latrotoxin), anti‐(α‐latroinsectotoxin) or anti‐(low‐molecular‐mass protein) IgG. Neither the low‐molecular‐mass protein nor α‐latrotoxin were toxic upon injection into Trichoplusia ni larvae or upon virus‐derived synthesis directly in the cytoplasm of the target tissue. Analysis of the biological activity of the recombinant virus encoding α‐latroinsectotoxin, however, revealed a strong toxic effect on the T. ni larvae. These data indicate that the toxic effect of the native insectotoxin may be promoted by the α‐latroinsectotoxin subunit alone and provides evidence that the mechanism of action of α‐latroinsectotoxin may be mediated by internalisation of part of the neurotoxin α‐subunit molecule.

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Neurexins

Cited by 21 publications

References 0 publications

Binding Properties of Neuroligin 1 and Neurexin 1β Reveal Function as Heterophilic Cell Adhesion Molecules

Binding Properties of Neuroligin 1 and Neurexin 1β Reveal Function as Heterophilic Cell Adhesion Molecules

α‐Latrotoxin receptor

Functional Characterization of Black Widow Spider Neurotoxins Synthesised in Insect Cells

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