Presynaptic Expression of LRIT3 Transsynaptically Organizes the Postsynaptic Glutamate Signaling Complex Containing TRPM1. Cell Rep 2019 Jun 11;27(11):3107-3116.e3
Date
06/13/2019Pubmed ID
31189098Pubmed Central ID
PMC6628893DOI
10.1016/j.celrep.2019.05.056Scopus ID
2-s2.0-85066800714 (requires institutional sign-in at Scopus site) 30 CitationsAbstract
Throughout the CNS, interactions between pre- and postsynaptic adhesion molecules establish normal synaptic structure and function. Leucine-rich repeat (LRR) domain-containing proteins are a large family that has a diversity of ligands, and their absence can cause disease. At the first retinal synapse, the absence of LRIT3 expression leads to the disassembly of the postsynaptic glutamate signaling complex (signalplex) expressed on depolarizing bipolar cell (DBC) dendrites. The prevalent view is that assembly of the signalplex results from direct postsynaptic protein:protein interactions. In contrast, we demonstrate that LRIT3 is expressed presynaptically, in rod photoreceptors (rods), and when we restore LRIT3 expression in Lrit3-/- rods, we restore expression of the postsynaptic glutamate signalplex and rod-driven vision. Our results demonstrate that, in the retina, the LRR-containing protein LRIT3 acts as a transsynaptic organizer of the postsynaptic complex required for normal synaptic function.
Author List
Hasan N, Pangeni G, Cobb CA, Ray TA, Nettesheim ER, Ertel KJ, Lipinski DM, McCall MA, Gregg RGAuthor
Daniel M. Lipinski PhD Associate Professor in the Ophthalmology and Visual Sciences department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
AnimalsDendrites
Female
Glutamic Acid
Male
Membrane Proteins
Mice
Mice, Inbred C57BL
Retinal Bipolar Cells
Retinal Rod Photoreceptor Cells
Synapses
Synaptic Potentials
TRPM Cation Channels
