Phosphorylation of glutamate receptors: a potential mechanism for the regulation of receptor function and psychostimulant action.

Phosphorylation of glutamate receptors: a potential mechanism for the regulation of receptor function and psychostimulant action. Research Abstract Details 

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Phosphorylation of glutamate receptors: a potential mechanism for the regulation of receptor function and psychostimulant action. Abstract Text:

John Q Wang,Xianyu Liu,Guochi Zhang,Nikhil K Parelkar,Anish Arora,Michelle Haines,Eugene E Fibuch,Limin Mao,

Ionotropic glutamate receptors, N-methyl-d-aspartate receptors (NMDARs) and alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptors (AMPARs), are densely distributed in the mammalian brain and actively regulate a variety of cellular activities. Expression and function of these receptors are also under a tight regulation by many molecular mechanisms. Protein phosphorylation represents one of the important mechanisms for the posttranslational modulation of these receptors. Constitutive and regulatory phosphorylation occurs at distinct sites (serine, threonine, or tyrosine) on the intracellular C-terminal domain of almost all subunits capable of assembling a functional channel. Several key protein kinases, such as protein kinase A, protein kinase C, Ca(2+)/calmodulin-dependent protein kinases, and tyrosine kinases are involved in the site-specific catalyzation and regulation of NMDAR and AMPAR phosphorylation. Through the phosphorylation mechanism, these protein kinases as well as protein phosphatases control biochemical properties (biosynthesis, delivery, and subunit assembling), subcellular distribution, and interactions of these receptors with various synaptic proteins, which ultimately modify the efficacy and strength of excitatory synapses containing NMDARs and AMPARs and many forms of synaptic plasticity. Emerging evidence shows that psychostimulants (cocaine and amphetamine) are among effective agents that profoundly alter the phosphorylation status of both receptors in striatal neurons in vivo. Thus, psychostimulants may modulate NMDAR and AMPAR function through the phosphorylation mechanism to shape the excitatory synaptic plasticity related to additive properties of drugs of abuse.

Phosphorylation of glutamate receptors: a potential mechanism for the regulation of receptor function and psychostimulant action. Publishing Authors By Initials

JQ Wang,X Liu,G Zhang,NK Parelkar,A Arora,M Haines,EE Fibuch,L Mao,

For similar proteins: membrane proteins: receptors, cell surface: receptors, neurotransmitter: receptors, amino acid: receptors, glutamate research abstracts see: proteins: membrane proteins: receptors, cell surface: receptors, neurotransmitter: receptors, amino acid: receptors, glutamate research

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Phosphorylation of glutamate receptors: a potential mechanism for the regulation of receptor function and psychostimulant action. Journal Published:

PUBLICATION TYPE: Review

Journal: Journal of neuroscience research

VOLUME: 84

Page Numbers: 1621-9

Journal Abbreviation: J. Neurosci. Res.

ISSN: 0360-4012

DAY: 3

MONTH: Dec

YEAR: 2006

Phosphorylation of glutamate receptors: a potential mechanism for the regulation of receptor function and psychostimulant action. Information

Number of References: 73

LANGUAGE: eng

NlmUniqueID: 7600111

Phosphorylation of glutamate receptors: a potential mechanism for the regulation of receptor function and psychostimulant action. Keywords Mesh Terms:

KEYWORDS: Receptors, Glutamate

MESH TERMS: metabolism

Chemical & Substance for Abstract: Phosphorylation of glutamate receptors: a potential mechanism for the regulation of receptor function and psychostimulant action. Information

Substance Name: Protein Kinases

Registry Number: EC 2.7.1.37

Grant and Affiliation Information for Phosphorylation of glutamate receptors: a potential mechanism for the regulation of receptor function and psychostimulant action.

AFFILIATION: Department of Basic Medical Science, University of Missouri-Kansas City, School of Medicine, Kansas City, MO, USA. wangjq@umkc.edu

Country: United States

AGENCY: United States NIMH

GRANT: R01-MH61469

ACRONYM: MH

MEDLINETA: J Neurosci Res

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