TY - JOUR
T1 - Phosphorylation of amino acid neurotransmitter receptors in synaptic plasticity
AU - Raymond, Lynn A.
AU - Blackstone, Craig D.
AU - Huganir, Richard L.
PY - 1993/4
Y1 - 1993/4
N2 - The precise regulation of synaptic efficacy in the mammalian central nervous system is fundamental for learning, memory, motor control and sensory processing, as well as synaptogenesis. Currently, the molecular mechanisms underlying synaptic plasticity involved in these crucial processes are topics of intense investigation. The modulation of neurotransmitter receptors has received considerable attention, since these receptors mediate signal transduction at the postsynaptic membranes of chemical synapses. Over the past several years, evidence has suggested that protein phosphorylation of neurotransmitter receptors is a common mechanism for the regulation of receptor function. In this reaction, protein kinases catalyse the transfer of a highly charged phosphate moiety from ATP to serine, threonine or tyrosine residues of a neurotransmitter receptor, thereby altering the charge and/or conformation of the receptor and regulating its function. Phosphorylation of neurotransmitter receptors is reversible, can occur rapidly, and might result in prolonged changes in receptor function. Thus, this modification might play an important role in both short- and long-term changes in synaptic transmission.
AB - The precise regulation of synaptic efficacy in the mammalian central nervous system is fundamental for learning, memory, motor control and sensory processing, as well as synaptogenesis. Currently, the molecular mechanisms underlying synaptic plasticity involved in these crucial processes are topics of intense investigation. The modulation of neurotransmitter receptors has received considerable attention, since these receptors mediate signal transduction at the postsynaptic membranes of chemical synapses. Over the past several years, evidence has suggested that protein phosphorylation of neurotransmitter receptors is a common mechanism for the regulation of receptor function. In this reaction, protein kinases catalyse the transfer of a highly charged phosphate moiety from ATP to serine, threonine or tyrosine residues of a neurotransmitter receptor, thereby altering the charge and/or conformation of the receptor and regulating its function. Phosphorylation of neurotransmitter receptors is reversible, can occur rapidly, and might result in prolonged changes in receptor function. Thus, this modification might play an important role in both short- and long-term changes in synaptic transmission.
UR - http://www.scopus.com/inward/record.url?scp=0027403322&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0027403322&partnerID=8YFLogxK
U2 - 10.1016/0166-2236(93)90123-4
DO - 10.1016/0166-2236(93)90123-4
M3 - Review article
C2 - 7682348
AN - SCOPUS:0027403322
SN - 0166-2236
VL - 16
SP - 147
EP - 153
JO - Trends in neurosciences
JF - Trends in neurosciences
IS - 4
ER -