ArticleFrontiers in molecular neuroscience2016
The Mechanism of Regulated Release of Lasso/Teneurin-2.
Article in Frontiers in molecular neuroscience, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 37 citations in OpenAlex.
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- A multi-omic single-cell landscape of cellular diversification in the developing human cerebral cortex.Computational and structural biotechnology journal · 2024Article
- Molecular and functional profiling of cell diversity and identity in the lateral superior olive, an auditory brainstem center with ascending and descending projections.Frontiers in cellular neuroscience · 2024Article
- A novel role for Teneurin C-terminal Associated Peptide (TCAP) in the regulation of cardiac activity in the Sydney rock oyster,Frontiers in endocrinology · 2023Article
- The Cannabis-Induced Epigenetic Regulation of Genes Associated with Major Depressive Disorder.Genes · 2022Review
- ADGRL1 haploinsufficiency causes a variable spectrum of neurodevelopmental disorders in humans and alters synaptic activity and behavior in a mouse model.American journal of human genetics · 2022Article
- Teneurin4 dimer structures reveal a calcium-stabilized compact conformation supporting homomeric trans-interactions.The EMBO journal · 2022Article
- Teneurin paralogues are able to localise synaptic sites driven by the intracellular domain and have the potential to formFrontiers in neuroscience · 2022Article
- Poorer Well-Being in Children With Misophonia: Evidence From theFrontiers in psychology · 2022Article
- To Stick or Not to Stick: The Multiple Roles of Cell Adhesion Molecules in Neural Circuit Assembly.Frontiers in neuroscience · 2022Review
- Alternative splicing controls teneurin-latrophilin interaction and synapse specificity by a shape-shifting mechanism.Nature communications · 2020Article
- Mechanistic advances in axon pathfinding.Current opinion in cell biology · 2020Review
- The expanding functional roles and signaling mechanisms of adhesion G protein-coupled receptors.Annals of the New York Academy of Sciences · 2019Article
- Beyond the Ligand: Extracellular and Transcellular G Protein-Coupled Receptor Complexes in Physiology and Pharmacology.Pharmacological reviews · 2019Review
- Teneurins and latrophilins: two giants meet at the synapse.Current opinion in structural biology · 2019Review
- Activity of the Carboxy-Terminal Peptide Region of the Teneurins and Its Role in Neuronal Function and Behavior in Mammals.Frontiers in neuroscience · 2019Review
- The Tenets of Teneurin: Conserved Mechanisms Regulate Diverse Developmental Processes in theFrontiers in neuroscience · 2019Article
- Teneurin C-Terminal Associated Peptide (TCAP)-1 and Latrophilin Interaction in HEK293 Cells: Evidence for Modulation of Intercellular Adhesion.Frontiers in endocrinology · 2019Article
- Latrophilins and Teneurins in Invertebrates: No Love for Each Other?Frontiers in neuroscience · 2019Review
- Expression and Roles of Teneurins in Zebrafish.Frontiers in neuroscience · 2019Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Teneurins are large cell-surface receptors involved in axon guidance. Teneurin-2 (also known as latrophilin-1-associated synaptic surface organizer (Lasso)) interacts across the synaptic cleft with presynaptic latrophilin-1, an adhesion G-protein-coupled receptor that participates in regulating neurotransmitter release. Lasso-latrophilin-1 interaction mediates synapse formation and calcium signaling, highlighting the important role of this trans-synaptic receptor pair. However, Lasso is thought to be proteolytically cleaved within its ectodomain and released into the medium, making it unclear whether it acts as a proper cell-surface receptor or a soluble protein. We demonstrate here that during its intracellular processing Lasso is constitutively cleaved at a furin site within its ectodomain. The cleaved fragment, which encompasses almost the entire ectodomain of Lasso, is potentially soluble; however, it remains anchored on the cell surface via its non-covalent interaction with the transmembrane fragment of Lasso. Lasso is also constitutively cleaved within the intracellular domain (ICD). Finally, Lasso can be further proteolytically cleaved within the transmembrane domain. The third cleavage is regulated and releases the entire ectodomain of Lasso into the medium. The released ectodomain of Lasso retains its functional properties and binds latrophilin-1 expressed on other cells; this binding stimulates intracellular Ca(2+) signaling in the target cells. Thus, Lasso not only serves as a bona fide cell-surface receptor, but also as a partially released target-derived signaling factor.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.