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Metabotropic glutamate receptor 1 recycles to the cell surface in protein phosphatase 2A‐dependent manner in non‐neuronal and neuronal cell lines
Author(s) -
Pandey Saurabh,
Mahato Prabhat Kumar,
Bhattacharyya Samarjit
Publication year - 2014
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/jnc.12930
Subject(s) - metabotropic glutamate receptor , metabotropic glutamate receptor 1 , microbiology and biotechnology , metabotropic glutamate receptor 7 , metabotropic receptor , internalization , receptor , metabotropic glutamate receptor 6 , biology , endocytosis , metabotropic glutamate receptor 5 , metabotropic glutamate receptor 3 , glutamate receptor , phosphatase , synaptic plasticity , metabotropic glutamate receptor 4 , neuroscience , biochemistry , phosphorylation
Trafficking of G protein‐coupled receptors plays a crucial role in controlling the precise signalling of the receptor as well as its proper regulation. Metabotropic glutamate receptor 1 ( mG luR1), a G protein‐coupled receptor, is a member of the group I mG luR family. mG luR1 plays a critical role in neuronal circuit formation and also in multiple types of synaptic plasticity. This receptor has also been reported to be involved in various neuropsychiatric diseases. Other than the central nervous system, mG luR1 plays crucial roles in various non‐neuronal cells like hepatocytes, skin cells, etc. Although it has been reported that mG luR1 gets endocytosed on ligand application, the events after the internalization of the receptor has not been studied. We show here that mG luR1 internalizes on ligand application. Subsequent to endocytosis, majority of the receptors localize at the recycling compartment and no significant presence of the receptor was noticed in the lysosome. Furthermore, mG luR1 returned to the cell membrane subsequent to ligand‐mediated internalization. We also show here that the recycling of mG luR1 is dependent on the activity of protein phosphatase 2A. Thus, our data suggest that the ligand‐mediated internalized receptors recycle back to the cell surface in protein phosphatase 2A‐dependent manner.Metabotropic glutamate receptor 1 mGluR1 is involved in various forms of synaptic plasticity and in many neuropsychiatric disorders. We show here that mGluR1 internalizes on ligand application and subsequently recycles to the cell surface. Our data also suggest that inhibition of protein phosphatase PP2A activity completely inhibits the recycling of mGluR1. Thus, our data provide important information regarding the trafficking of mGluR1 to help us understand the regulation of the receptor in both the normal and diseased brain.