PMID- 10366608
OWN - NLM
STAT- MEDLINE
DCOM- 19990628
LR  - 20210218
IS  - 1529-2401 (Electronic)
IS  - 0270-6474 (Linking)
VI  - 19
IP  - 12
DP  - 1999 Jun 15
TI  - Characterization of phosphorylation sites on the glutamate receptor 4 subunit of 
      the AMPA receptors.
PG  - 4748-54
AB  - Recent studies have suggested that protein phosphorylation of glutamate receptors
      may play an important role in synaptic transmission. Specifically, the
      phosphorylation of AMPA receptors has been implicated in cellular models of
      synaptic plasticity. The phosphorylation of the glutamate receptor 1 (GluR1)
      subunit of AMPA receptors by protein kinase A (PKA), protein kinase C (PKC), and 
      Ca2+/calmodulin-dependent protein kinase II (CaMKII) has been characterized
      extensively. Phosphorylation of this subunit occurs exclusively on the
      intracellular C-terminal domain. However, the GluR1 subunit C terminus shows low 
      homology to the other AMPA receptor subunits. In this paper we characterized the 
      phosphorylation of AMPA receptor subunit GluR4, using site-specific mutagenesis
      and biochemical techniques. We found that GluR4 is phosphorylated on serine 842
      within the C-terminal domain in vitro and in vivo. Serine 842 is phosphorylated
      by PKA, PKC, and CaMKII in vitro and is phosphorylated in transfected cells by
      PKA. Two-dimensional phosphopeptide analysis indicates that serine 842 is the
      major phosphorylation site on GluR4. In addition, we identified threonine 830 as 
      a potential PKC phosphorylation site. These results suggest that GluR4, which is 
      the most rapidly desensitizing AMPA receptor subunit, may be modulated by
      phosphorylation.
FAU - Carvalho, A L
AU  - Carvalho AL
AD  - Center for Neuroscience of Coimbra, Department of Biochemistry, University of
      Coimbra, 3000 Coimbra, Portugal.
FAU - Kameyama, K
AU  - Kameyama K
FAU - Huganir, R L
AU  - Huganir RL
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Neurosci
JT  - The Journal of neuroscience : the official journal of the Society for
      Neuroscience
JID - 8102140
RN  - 0 (Receptors, AMPA)
RN  - 0 (glutamate receptor ionotropic, AMPA 4)
RN  - 1F7A44V6OU (Colforsin)
RN  - 2ZD004190S (Threonine)
RN  - 3KX376GY7L (Glutamic Acid)
RN  - EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinases)
RN  - EC 2.7.11.13 (Protein Kinase C)
RN  - EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinase Type 2)
RN  - EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Binding Sites/drug effects/physiology
MH  - Calcium-Calmodulin-Dependent Protein Kinase Type 2
MH  - Calcium-Calmodulin-Dependent Protein Kinases/metabolism/pharmacology
MH  - Cell Line
MH  - Colforsin/pharmacology
MH  - Cyclic AMP-Dependent Protein Kinases/metabolism/pharmacology
MH  - Epithelial Cells/chemistry/cytology/enzymology
MH  - Glutamic Acid/*metabolism
MH  - Humans
MH  - Kidney/cytology
MH  - Molecular Sequence Data
MH  - Mutagenesis/physiology
MH  - Phosphorylation
MH  - Protein Kinase C/metabolism/pharmacology
MH  - *Receptors, AMPA/chemistry/genetics/metabolism
MH  - Synaptic Transmission/physiology
MH  - Threonine/metabolism
MH  - Transfection
PMC - PMC6782640
EDAT- 1999/06/15 00:00
MHDA- 1999/06/15 00:01
CRDT- 1999/06/15 00:00
PHST- 1999/06/15 00:00 [pubmed]
PHST- 1999/06/15 00:01 [medline]
PHST- 1999/06/15 00:00 [entrez]
PST - ppublish
SO  - J Neurosci. 1999 Jun 15;19(12):4748-54.