Latrophilins Function as Heterophilic Cell-adhesion Molecules by Binding to Teneurins

Boucard, Antony A.; Maxeiner, Stephan; Südhof, Thomas C.

doi:10.1074/jbc.m113.504779

Cited by 174 publications

(336 citation statements)

References 49 publications

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“…As for LPHN3 mRNA brain expression, its peak was observed immediately after birth, followed by a decrease, similar to LPHN2 mRNA decay pattern. In contrast, real-time quantitative PCR done with mouse brain tissues demonstrated that the expression profile of LPHN3 mRNA mimicked LPHN1 pattern, while LPHN2 behaved differently: both LPHN1 and LPHN3 mRNA levels increased after birth reaching a plateau during the period describing intense synaptogenesis, while LPHN2 mRNA levels underwent a constant decrease (34,37). As the function of LPHN seems tightly linked to the development of neuronal tissue, these data suggest that each LPHN isoform may contribute differently in shaping neuronal networks.…”

Section: Developmental Regulation Of Lphn Expressionmentioning

confidence: 53%

“…This conclusion was reached since the lectin-like domain had very low affinity for rhamnose. This suspicion turned out to be supported by interaction of the lectin-like domain with the newly identified TEN (37,47). These ligands will be discussed in the "Latrophilin ligands and associated functions" section.…”

Section: The Ntf the Lectin-like Domainmentioning

confidence: 94%

“…Splicing will therefore generate different isoforms for LPHN with possibly different functions. Indeed, splice site A insert affects LPHN1 affinity for TEN but does not significantly change its affinity for either NRXN or FLRT3, two endogenous ligands of LPHN (37). This mechanism is susceptible to affect ligand selection in a neuronal network where LPHN establish a specific interaction pattern with its different ligands.…”

Section: The Extracellular Alternatively Splice Insert Amentioning

confidence: 96%

“…This suggested that the lectin-like domain was not fully recapitulating the binding pocket, but that it was sufficient for LPHN/TEN interaction. In mouse neuronal cultures, this interaction regulates the maintenance or formation of both excitatory and inhibitory synapses (37). Evolutionary speaking, the lectin-like domain is present in all vertebrate and invertebrate LPHN, thus, seems to have a conserved function in these organisms (27).…”

Section: The Ntf the Lectin-like Domainmentioning

confidence: 99%

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Latrophilins updated

Meza-Aguilar

Boucard

2014

Biomolecular Concepts

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Latrophilins (LPHN) are part of a yet unexplored family of receptors comprising three isoforms, LPHN1-3, and belonging to a unique branch of G protein-coupled receptors (GPCR) named adhesion GPCR (aGPCR). LPHN are considered to be prototypical models for the study of aGPCR as they are one of the most evolutionary conserved members. Previously described as the target for a potent neurotoxin from the black widow spider venom, LPHN are now being studied under a whole new perspective. Indeed, recent advances have provided a better understanding of different aspects of this prototypical family of receptors: 1) elucidation of LPHN ectodomain organization by crystallography has unveiled a new functional domain with great repercussion on all the other members of the aGPCR family, 2) proteomic approaches have opened the gate to unsuspected functional characteristics of LPHN cellular role, and 3) genetic approaches have provided hints into the physiological functions of LPHN in specific systems and organisms. Moreover, genomic linkage studies screening human patients from diverse genetic backgrounds have involved LPHN gene defects in human disorders such as attention-deficit hyperactivity disorder and cancer. In this review, we will provide a historical perspective addressing experimental research on these receptors while highlighting the new advances and discoveries concerning LPHN functions. As GPCR still represent the most studied targets for the development of pharmacological approaches aiming at alleviating human disorders, the relevance of studying LPHN retains a high pertinence to better understand these receptors for the treatment of human diseases.

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Section: Developmental Regulation Of Lphn Expressionmentioning

confidence: 53%

Section: The Ntf the Lectin-like Domainmentioning

confidence: 94%

Section: The Extracellular Alternatively Splice Insert Amentioning

confidence: 96%

Section: The Ntf the Lectin-like Domainmentioning

confidence: 99%

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Latrophilins updated

Meza-Aguilar

Boucard

2014

Biomolecular Concepts

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“…Following the transmembrane domain, many teneurins have furin cleavage sites (20) preceding eight EGF repeats, through which teneurins can dimerize due to free cysteines in repeats 2 and 5 forming interchain disulfide bonds (5,21). The following NHL repeat domain is a predicted ␤-propeller and is responsible for homophilic rather than heterophilic interactions in some teneurins (5,22), although heterophilic interactions have also been observed (23). Interestingly, these interactions can lead to the release of the ECD (11,24).…”

mentioning

confidence: 99%

The Intracellular Domain of Teneurin-1 Induces the Activity of Microphthalmia-associated Transcription Factor (MITF) by Binding to Transcriptional Repressor HINT1

Schöler

Ferralli

Thiry

et al. 2015

Journal of Biological Chemistry

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Background:The intracellular domain of teneurins translocates to the nucleus and is thought to influence transcription. Results: The teneurin-1 intracellular domain binds the transcriptional repressor HINT1 and induces MITF target genes. Conclusion:The teneurin-1 intracellular domain prevents HINT1 from repressing MITF at its target gene promoters. Significance: This is a novel mechanism for a teneurin-mediated transcriptional control.

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Information Processing in Affective Disorders: Did an Ancient Peptide Regulating Intercellular Metabolism Become Co‐Opted for Noxious Stress Sensing?

Lovejoy

Hogg

2020

BioEssays

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Affective disorders arise in stressful situations from aberrant sensory information integration that affects energetic nutrient (i.e., glucose) utilization to the cognitive centers of the brain. Because energy flow is mediated by molecular signals and receptors that evolved before the first complex brains, the phylogenetically oldest signaling systems are essential in the etiology of affective disorders. The corticotropin‐releasing factor (CRF) peptide subfamily is a phylogenetically old metazoan peptide family and is pivotal for regulating organismal energy response associated with stress. Highly conserved, both the CRF peptide family and its receptors possess a structural relationship to the teneurins, and their receptors, latrophilins, respectively. The CRF homologous region of teneurin is defined as the “teneurin C‐terminal associated peptide” (TCAP) and antagonizes CRF action, regulates mitochondrial energy production, and is anxiolytic in vivo. Here, it is postulated that TCAP represents an ancient peptide that mediates intercellular information transfer of stressful and noxious events by regulating energy utilization among neurons.

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Latrophilins Function as Heterophilic Cell-adhesion Molecules by Binding to Teneurins

Cited by 174 publications

References 49 publications

Latrophilins updated

Latrophilins updated

The Intracellular Domain of Teneurin-1 Induces the Activity of Microphthalmia-associated Transcription Factor (MITF) by Binding to Transcriptional Repressor HINT1

Information Processing in Affective Disorders: Did an Ancient Peptide Regulating Intercellular Metabolism Become Co‐Opted for Noxious Stress Sensing?

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