{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lee S"],"funding":["Korea Dementia Research Center","National Research Foundation of Korea (NRF)","Korea Dementia Research Center (KDRC)","National Research Foundation of Korea"],"pagination":["e2316819121"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11066993"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["121(18)"],"pubmed_abstract":["Posttranslational modifications regulate the properties and abundance of synaptic α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors that mediate fast excitatory synaptic transmission and synaptic plasticity in the central nervous system. During long-term depression (LTD), protein tyrosine phosphatases (PTPs) dephosphorylate tyrosine residues in the C-terminal tail of AMPA receptor GluA2 subunit, which is essential for GluA2 endocytosis and group I metabotropic glutamate receptor (mGluR)-dependent LTD. However, as a selective downstream effector of mGluRs, the mGluR-dependent PTP responsible for GluA2 tyrosine dephosphorylation remains elusive at Schaffer collateral (SC)-CA1 synapses. In the present study, we find that mGluR5 stimulation activates Src homology 2 (SH2) do"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["SHP2 regulates GluA2 tyrosine phosphorylation required for AMPA receptor endocytosis and mGluR-LTD."],"pmcid":["PMC11066993"],"funding_grant_id":["NRF-2020R1A5A1019023","NRF-2023R1A2C2003229","NRF-2022R1A2C1004913","NRF-2018R1A5A2025964","HU21C0071","NRF-2018R1A2B6004759"],"pubmed_authors":["Lee YS","Lee S","Song JM","Jang H","Kim J","Suh YH","Ryu HH","Lee D"],"additional_accession":[]},"is_claimable":false,"name":"SHP2 regulates GluA2 tyrosine phosphorylation required for AMPA receptor endocytosis and mGluR-LTD.","description":"Posttranslational modifications regulate the properties and abundance of synaptic α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors that mediate fast excitatory synaptic transmission and synaptic plasticity in the central nervous system. During long-term depression (LTD), protein tyrosine phosphatases (PTPs) dephosphorylate tyrosine residues in the C-terminal tail of AMPA receptor GluA2 subunit, which is essential for GluA2 endocytosis and group I metabotropic glutamate receptor (mGluR)-dependent LTD. However, as a selective downstream effector of mGluRs, the mGluR-dependent PTP responsible for GluA2 tyrosine dephosphorylation remains elusive at Schaffer collateral (SC)-CA1 synapses. In the present study, we find that mGluR5 stimulation activates Src homology 2 (SH2) do","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Apr","modification":"2025-04-04T02:57:24.082Z","creation":"2025-04-04T02:57:24.082Z"},"accession":"S-EPMC11066993","cross_references":{"pubmed":["38657042"],"doi":["10.1073/pnas.2316819121"]}}