Mass spectrometrical identification of hippocampal NMDA receptor subunits NR1, NR2A-D and five novel phosphorylation sites on NR2A and NR2B

Journal of Proteome Research
Maryam GhafariGert Lubec

Abstract

The NMDA receptor (NMDA-R) is a key element in neural transmission and mediating a vast variety of physiological and pathological processes in the nervous system. It is well-known that phosphorylation is required for functioning of the NMDA-R, and we therefore decided to study this post-translational modification in subunits NR1 and NR2A-D. Immunoprecipitation with an antibody against NR1 was carried out from rat hippocampi and SDS-PAGEs were run. Bands were punched, destained, and digested with trypsin and chymotrypsin and peptides were identified by nano-LC-ESI-MS/MS using an ion trap (HCT). Proteins were identified using specific software. Phosphorylations were verified by phosphatase treatment and reanalysis by mass spectrometry. The NMDA-R subunits NR1 and 2A-D were identified. On NR2A, a novel phosphorylation site was observed at S511, and on NR2B, four novel phosphorylation sites were revealed at S886, S917, S1303, and S1323 by mass spectrometry and verified by phosphatase treatment with mass spectrometrical reanalysis. A series of NMDA-R phosphorylations have been reported and these serve different functions as receptor activation, localization, and protein-protein interactions. Herein, findings of novel phosphorylation...Continue Reading

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Citations

Oct 17, 2012·Proceedings of the National Academy of Sciences of the United States of America·Narkhyun BaeGert Lubec
Dec 3, 2013·European Journal of Pharmacology·John Q WangLi-Min Mao
Oct 3, 2012·Journal of Proteomics·Gangsoo JungGert Lubec
Aug 14, 2015·Amino Acids·Soheil Keihan FalsafiGert Lubec
May 9, 2014·Brain Structure & Function·Maryam GhafariGert Lubec
May 30, 2012·Analytical Biochemistry·Narkhyun BaeGert Lubec
Feb 18, 2017·ACS Chemical Neuroscience·Anthony J Baucum
Jul 7, 2017·Scientific Reports·Mark O CollinsJyoti S Choudhary

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