α-Latrotoxin Stimulates Exocytosis by the Interaction with a Neuronal G-Protein-Coupled Receptor

Krasnoperov, Valery; Bittner, Mary A.; Beavis, Ronald C.; Kuang, Yanan; Salnikow, Konstantin; Chepurny, Oleg G.; Little, Roger; Plotnikov, A.N.; Wu, Dianqing; Holz, Ronald W.; Petrenko, Alexander G.

doi:10.1016/s0896-6273(00)80332-3

Cited by 311 publications

(385 citation statements)

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“…The defining structural feature of all aGPCR is the GPCR proteolytic site (GPS) motif (Krasnoperov et al, 1997), a juxtamembrane sequence embedded within a larger GPCR-autoproteolysis-inducing (GAIN) domain (Arac et al, 2012), which promotes proteolytic cleavage of an aGPCR pro-receptor into a two-subunit heteromeric complex (Lin et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Characterization and functional study of a cluster of four highly conserved orphan adhesion‐GPCR in mouse

Prömel

Waller-Evans

Dixon

et al. 2012

Developmental Dynamics

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Background: Adhesion G protein-coupled receptors (aGPCR) constitute a structurally and functionally diverse class of seven-transmembrane receptor proteins. Although for some of the members important roles in immunology, neurology, as well as developmental biology have been suggested, most receptors have been poorly characterized. Results: We have studied evolution, expression, and function of an entire receptor group containing four uncharacterized aGPCR: Gpr110, Gpr111, Gpr115, and Gpr116. We show that the genomic loci of these four receptors are clustered tightly together in mouse and human genomes and that this cluster likely derives from a single common ancestor gene. Using transcriptional profiling on wild-type and knockout/LacZ reporter knockin mice strains, we have obtained detailed expression maps that show ubiquitous expression of Gpr116, co-expression of Gpr111 and Gpr115 in developing skin, and expression of Gpr110 in adult kidney. Loss of Gpr110, Gpr111, or Gpr115 function did not result in detectable defects, indicating that genes of this aGPCR group might function redundantly. Conclusions: The aGPCR cluster Gpr110, Gpr111, Gpr115, and Gpr116 developed from one common ancestor in vertebrates. Expression suggests a role in epithelia, and one can speculate about a possible redundant function of GPR111 and GPR115. Developmental Dynamics 241:1591-1602, 2012.V C 2012 Wiley Periodicals, Inc.

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Section: Introductionmentioning

confidence: 99%

Characterization and functional study of a cluster of four highly conserved orphan adhesion‐GPCR in mouse

Prömel

Waller-Evans

Dixon

et al. 2012

Developmental Dynamics

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“…For example, gliomedin is a type II transmembrane protein containing the olfactomedin domain in the carboxy-terminal extracellular region [10]. Latrophilins are calcium-independent, seven-transmembrane receptors for latrotoxin (CIRL1-CIRL3) with a large N-terminal extracellular part containing the olfactomedin domain [11][12][13][14][15].…”

Section: Introductionmentioning

confidence: 99%

Optimedin induces expression of N-cadherin and stimulates aggregation of NGF-stimulated PC12 cells

Lee

Tomarev

2007

Experimental Cell Research

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Optimedin, also known as olfactomedin 3, belongs to a family of olfactomedin domain-containing proteins. It is expressed in neural tissues and Pax6 is involved in the regulation of its promoter. To study possible effects of optimedin on the differentiation of neural cells, we produced stably transfected PC12 cell lines expressing optimedin under a tetracycline-inducible promoter. Cells expressing high levels of optimedin showed higher growth rates and stronger adhesion to the collagen extracellular matrix as compared with control PC12 cells. After stimulation with nerve growth factor (NGF), optimedin-expressing cells demonstrated elevated levels of N-cadherin, β-catenin, α-catenin, and occludin as compared with stimulated, control PC12 cells. Expression of optimedin induced Ca 2+ -dependent aggregation of NGF-stimulated PC12 cells and this aggregation was blocked by the expression of N-cadherin siRNA. Expression of optimedin also changed the organization of the actin cytoskeleton and inhibited neurite outgrowth in NGF-stimulated PC12 cells. We suggest that expression of optimedin stimulates the formation of adherent and tight junctions on the cell surface and this may play an important role in the differentiation of the brain and retina through the modulation of cytoskeleton organization, cell-cell adhesion and migration.

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“…This inhibitory effect of the lectin involves binding to a-latrotoxin receptors, which hampers the subsequent association of the toxin (Meldolesi, 1982). a-Latrotoxin stimulates neurotransmitter release via at least two different receptors, neurexin Ta, which binds alatrotoxin in a Ca2+ -dependent manner (Geppert et al, 1998), and a Ca 2+ -independent receptor of a-latrotoxin (CIRL), also named latrophilin (Krasnoperov et al, 1997;Lelianova et al, 1997). Both neurexin Ia (Ushkaryov et al, 1992) and CIRL/latrophilin (Krasnoperov et al, 1997;Lelianova et al, 1997) are glycoproteins and can thus bind lectins.…”

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confidence: 99%

Presynaptic Inhibition by Concanavalin A: Are α‐Latrotoxin Receptors Involved in Action Potential‐Dependent Transmitter Release?

Boehm

Huck

1998

Journal of Neurochemistry

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Abstract:Effects of concanavalin A on transmitter release were investigated in primary cultures of chick sympathetic neurons. The lectin reduced electrically evoked [ 3H]noradrenaline release by up to 30% with half-maximal inhibition at 0.16 bLM. Concanavalin A also reduced the release triggered by extracellular Ca2~in neurons depolarized by 25 mM Kõr rendered Ca2-permeable by the ionophore A231 87. The inhibitory action of concanavaIm A on electrically evoked release was additive to that of the a 2-adrenergic agonist UK 14,304. Inactivation of Gãnd GIG0 type G proteins by either cholera or pertussis toxin did not alter the inhibitory effect of the lectin. Concanavalin A failed to affect the resting membrane potential, action potential waveforms, or voltage-dependent K~and Ca 2~currents. In contrast, the lectin efficiently blocked both the Ca2-dependent and -independent alatrotoxin-induced transmitter release, but only when applied before the toxin. The reduction of electrically evoked, as well as a-latrotoxin-evoked, release by concanavalin A was attenuated in the presence of glucose and abolished by methyl a-D-mannopyranoside. The dimeric derivative, succinyl-concanavalin A, was significantly less active than tetrameric concanavalin A. In bovine adrenal chromaffin cells, which displayed only weak secretory responses to a-latrotoxin, concanavalin A failed to alter K~-evokedcatecholamine secretion. These results show that concanavalin A causes presynaptic inhibition in sym pathetic neurons and indicate that cross-linking of a-latrotoxin receptors may reduce action potential-dependent transmitter release. Key Words: Concanavalin A-a-Latrotoxin-Noradrenaline release-Chick sympathetic neurons-Bovine chromaffin cells-Presynaptic inhibition.

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α-Latrotoxin Stimulates Exocytosis by the Interaction with a Neuronal G-Protein-Coupled Receptor

Cited by 311 publications

References 73 publications

Characterization and functional study of a cluster of four highly conserved orphan adhesion‐GPCR in mouse

Characterization and functional study of a cluster of four highly conserved orphan adhesion‐GPCR in mouse

Optimedin induces expression of N-cadherin and stimulates aggregation of NGF-stimulated PC12 cells

Presynaptic Inhibition by Concanavalin A: Are α‐Latrotoxin Receptors Involved in Action Potential‐Dependent Transmitter Release?

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