BROWSE

Related Researcher

Author's Photo

Min, Kyung-Tai
Molecular & Cellular Neurobiology Lab(Min Lab)
Research Interests
  • adult neurogenesis; axon development; axon regeneration; protein stability; protein synthesis; Down syndrome; Alzheimer's disease;
  • learning and memory; mitochondria dynamics

ITEM VIEW & DOWNLOAD

Identification of a phosphorylation site for calcium/calmodulin-dependent protein kinase II in the NR2B subunit of the N-methyl-D-aspartate receptor

Cited 203 times inthomson ciCited 209 times inthomson ci
Title
Identification of a phosphorylation site for calcium/calmodulin-dependent protein kinase II in the NR2B subunit of the N-methyl-D-aspartate receptor
Author
Omkumar, RVKiely, MJRosenstein, AJMin, Kyung-TaiKennedy, MB
Keywords
POSTSYNAPTIC DENSITY PROTEIN; LONG-TERM POTENTIATION; GLUTATHIONE-S-TRANSFERASE; SPINAL-CORD NEURONS; NMDA RECEPTORS; GLUTAMATE RECEPTORS; HIPPOCAMPAL-NEURONS; CALCIUM; BRAIN; PURIFICATION
Issue Date
1996-12
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Citation
JOURNAL OF BIOLOGICAL CHEMISTRY, v.271, no.49, pp.31670 - 31678
Abstract
The N-methyl-D-aspartate (NMDA) subtype of excitatory glutamate receptors plays critical roles in embryonic and adult synaptic plasticity in the central nervous system. The receptor is a heteromultimer of core subunits, NR1, and one or more regulatory subunits, NR2A-D. Protein phosphorylation can regulate NMDA receptor function (Lieberman, D. N., and Mody, I. (1994) Nature 369, 235-239; Wang, Y. T., and Salter, M. W. (1994) Nature 369, 233-235; Wang, L.-Y., Orser, B. A., Brautigan, D. L., and MacDonald, J. F. (1994) Nature 369, 230-232). Here we identify a major phosphorylation site on subunit NR2B that is phosphorylated by Ca2+/calmodulin-dependent protein kinase II (CaM kinase II), an abundant protein kinase located at postsynaptic sites in glutamatergic synapses. For the initial identification of the site, we constructed a recombinant fusion protein containing 334 amino acids of the C terminus of the NR2B subunit and phosphorylated it with CaM kinase II in vitro. By peptide mapping, automated sequencing, and mass spectrometry, we identified the major site of phosphorylation on the fusion protein as Ser-383, corresponding to Ser-1303 of full-length NR2B. The K(m) for phosphorylation of this site in the fusion protein was ~50 nM, much lower than that of other known substrates for CaM kinase II, suggesting that the receptor is a high affinity substrate. We show that serine 1303 in the full-length NR2B and/or the cognate site in NR2A is a major site of phosphorylation of the receptor both in the postsynaptic density fraction and in living hippocampal neurons.
URI
Go to Link
DOI
10.1074/jbc.271.49.31670
ISSN
0021-9258
Appears in Collections:
BME_Journal Papers
Files in This Item:
2-s2.0-0029905992.pdf Download

find_unist can give you direct access to the published full text of this article. (UNISTARs only)

Show full item record

qrcode

  • mendeley

    citeulike

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

MENU