ArticleNature communications2020
Structural basis of liprin-α-promoted LAR-RPTP clustering for modulation of phosphatase activity.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
28 citing papers in PubMed, 45 citations in OpenAlex.
- Liprin-α family proteins and their cellular functions.The Journal of biological chemistry · 2026Review
- Synaptic Cell Adhesion: A Structural Perspective.Advances in neurobiology · 2026Review
- Telocytes deliver essential Wnts directly to murine intestinal stem cells via synapse-like contacts.Developmental cell · 2025Article
- Synaptic and Non-Synaptic Functions of PTPRD: A Receptor Tyrosine Phosphatase at the Crossroads of Neural Circuitry and Metabolism.Journal of neurochemistry · 2025Review
- Rare missense variants of the leukocyte common antigen related receptor (LAR) display reduced activity in transcellular adhesion and synapse formation.Research square · 2025Article
- The liprin-α/RIM complex regulates the dynamic assembly of presynaptic active zones via liquid-liquid phase separation.PLoS biology · 2025Article
- Rare missense variants of the leukocyte common antigen related receptor (LAR) display reduced activity in transcellular adhesion and synapse formation.bioRxiv : the preprint server for biology · 2025Article
- Distinct active zone protein machineries mediate CaNature neuroscience · 2024Article
- PTEN inhibition promotes robust growth of bulbospinal respiratory axons and partial recovery of diaphragm function in a chronic model of cervical contusion spinal cord injury.Experimental neurology · 2024Article
- The tyrosine phosphatases LAR and PTPRδ act as receptors of the nidogen-tetanus toxin complex.The EMBO journal · 2024Article
- Identification of the growth cone as a probe and driver of neuronal migration in the injured brain.Nature communications · 2024Article
- Molecular definition of distinct active zone protein machineries for CabioRxiv : the preprint server for biology · 2023Article
- The Structural Dynamics, Complexity of Interactions, and Functions in Cancer of Multi-SAM Containing Proteins.Cancers · 2023Review
- Enforced Dimerization of CD45 by the Adenovirus E3/49K Protein Inhibits T Cell Receptor Signaling.Journal of virology · 2023Article
- Article
- Bi-allelic loss-of-function variants in PPFIBP1 cause a neurodevelopmental disorder with microcephaly, epilepsy, and periventricular calcifications.American journal of human genetics · 2022Article
- Cytoneme-like protrusion formation induced by LAR is promoted by receptor dimerization.Biology open · 2022Article
- PPFIA4 promotes castration-resistant prostate cancer by enhancing mitochondrial metabolism through MTHFD2.Journal of experimental & clinical cancer research : CR · 2022Article
- Article
- Liprins in oncogenic signaling and cancer cell adhesion.Oncogene · 2021Review
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Leukocyte common antigen-related receptor protein tyrosine phosphatases (LAR-RPTPs) are cell adhesion molecules involved in mediating neuronal development. The binding of LAR-RPTPs to extracellular ligands induces local clustering of LAR-RPTPs to regulate axon growth and synaptogenesis. LAR-RPTPs interact with synaptic liprin-α proteins via the two cytoplasmic phosphatase domains, D1 and D2. Here we solve the crystal structure of LAR_D1D2 in complex with the SAM repeats of liprin-α3, uncovering a conserved two-site binding mode. Cellular analysis shows that liprin-αs robustly promote clustering of LAR in cells by both the liprin-α/LAR interaction and the oligomerization of liprin-α. Structural analysis reveals a unique homophilic interaction of LAR via the catalytically active D1 domains. Disruption of the D1/D1 interaction diminishes the liprin-α-promoted LAR clustering and increases tyrosine dephosphorylation, demonstrating that the phosphatase activity of LAR is negatively regulated by forming clusters. Additionally, we find that the binding of LAR to liprin-α allosterically regulates the liprin-α/liprin-β interaction.
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Registered trials
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.