ArticleThe Journal of comparative neurology2021
LRRTM4 is a member of the transsynaptic complex between rod photoreceptors and bipolar cells.
Article in The Journal of comparative neurology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- A decade of progress in understanding LRRTM and Slitrk synaptic cell-adhesion molecules.Molecules and cells · 2026Review
- Neuron-specific transcriptomic dysregulation in methotrexate-induced cognitive impairment revealed by SnRNA-seq.International journal of surgery (London, England) · 2026Article
- Trans-synaptic Interaction with mGluR6 Contributes to ELFN1 Presynaptic Enrichment in Rod Photoreceptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025Article
- Single-nucleus profiling decoding the subcortical visual pathway evolution of vertebrates.iScience · 2025Article
- Defective glycosylation and ELFN1 binding of mGluR6 congenital stationary night blindness mutants.Life science alliance · 2025Article
- Dystroglycan-HSPG interactions provide synaptic plasticity and specificity.Glycobiology · 2024Review
- Lnc-LRRTM4 promotes proliferation, metastasis and EMT of colorectal cancer through activating LRRTM4 transcription.Cancer cell international · 2023Article
- LRIT3 expression in cone photoreceptors restores post-synaptic bipolar cell signalplex assembly and partial function iniScience · 2023Article
- Trophoblast glycoprotein is required for efficient synaptic vesicle exocytosis from retinal rod bipolar cells.Frontiers in cellular neuroscience · 2023Article
- LRRTM3 regulates activity-dependent synchronization of synapse properties in topographically connected hippocampal neural circuits.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Leucine rich repeat transmembrane (LRRTM) proteins are synaptic adhesion molecules with roles in synapse formation and signaling. LRRTM4 transcripts were previously shown to be enriched in rod bipolar cells (BCs), secondary neurons of the retina that form synapses with rod photoreceptors. Using two different antibodies, LRRTM4 was found to reside primarily at rod BC dendritic tips, where it colocalized with the transduction channel protein, TRPM1. LRRTM4 was not detected at dendritic tips of ON-cone BCs. Following somatic knockout of LRRTM4 in BCs by subretinal injection and electroporation of CRISPR/Cas9, LRRTM4 was abolished or reduced in the dendritic tips of transfected cells. Knockout cells had a normal complement of TRPM1 at their dendritic tips, while GPR179 accumulation was partially reduced. In experiments with heterologously expressed protein, the extracellular domain of LRRTM4 was found to engage in heparan-sulfate dependent binding with pikachurin. These results implicate LRRTM4 in the GPR179-pikachurin-dystroglycan transsynaptic complex at rod synapses.
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