LRRTM4 is a member of the transsynaptic complex between rod photoreceptors and bipolar cells.

LRRTM4 RRID: CVCL_0045 RRID: IMSR_CRL:22 RRID:AB_2138196 RRID:AB_2284227 RRID:AB_2336642 RRID:Addgene_18817 RRID:Addgene_59313 pikachurin rod bipolar cell rod photoreceptor synaptic adhesion molecule

Journal

The Journal of comparative neurology
ISSN: 1096-9861
Titre abrégé: J Comp Neurol
Pays: United States
ID NLM: 0406041

Informations de publication

Date de publication:
01 2021
Historique:
received: 17 02 2020
revised: 09 04 2020
accepted: 01 05 2020
pubmed: 12 5 2020
medline: 17 12 2021
entrez: 12 5 2020
Statut: ppublish

Résumé

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.

Identifiants

pubmed: 32390181
doi: 10.1002/cne.24944
pmc: PMC7652719
mid: NIHMS1591364
doi:

Substances chimiques

LRRTM4 protein, mouse 0
Membrane Proteins 0
Nerve Tissue Proteins 0

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

221-233

Subventions

Organisme : NEI NIH HHS
ID : R01 EY025218
Pays : United States
Organisme : NEI NIH HHS
ID : R01 EY026545
Pays : United States

Informations de copyright

© 2020 Wiley Periodicals LLC.

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Auteurs

Melina A Agosto (MA)

Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas, USA.

Theodore G Wensel (TG)

Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas, USA.

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