Modulation of amino acid-gated ion channels by protein phosphorylation

被引:113
作者
Moss, Stephen J.
Smart, Trevor G.
机构
[1] UCL, MRC, Mol Cell Biol Lab, London WC1E 6BT, England
[2] UCL, Dept Pharmacol, London WC1E 6BT, England
[3] Univ London, Sch Pharm, Dept Pharmacol, London WC1N 1AX, England
来源
INTERNATIONAL REVIEW OF NEUROBIOLOGY, VOL 39 | 1996年 / 39卷
关键词
D O I
10.1016/S0074-7742(08)60662-5
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
The major excitatory and inhibitory amino acid receptors in the mammalian central nervous system are considered to be glutamate, gamma-aminobutyric acid type A (GABA(A)), and glycine receptors. These receptors are widely acknowledged to participate in fast synaptic neurotransmission, which ultimately is responsible for the control of neuronal excitability. In addition to these receptors being regulated by endogenous factors, including the natural neurotransmitters, they also form target substrates for phosphorylation by a number of protein kinases, including serine/threonine and tyrosine kinases. The process of phosphorylation involves the transfer of a phosphate group(s) from adenosine triphosphate to one or more serine, threonine, or tyrosine residues, which are invariably found in an intracellular location within the receptor. Phosphorylation is an important means of receptor regulation since it represents a covalent modification of the receptor structure, which can have important implications for ion channel function. This chapter reviews the current molecular and biochemical evidence regarding the sites of phosphorylation for both native neuronal and recombinant glutamate, GABA(A) and glycine receptors, and also reviews the functional electrophysiological implications of phosphorylation for receptor function.
引用
收藏
页码:1 / 52
页数:52
相关论文
共 189 条
[1]   PROTEIN-KINASE A-MEDIATED PHOSPHORYLATION REDUCES ONLY THE FAST DESENSITIZING GLYCINE CURRENT IN ACUTELY DISSOCIATED VENTROMEDIAL HYPOTHALAMIC NEURONS [J].
AGOPYAN, N ;
TOKUTOMI, N ;
AKAIKE, N .
NEUROSCIENCE, 1993, 56 (03) :605-615
[2]   CLONING OF A GLYCINE RECEPTOR SUBTYPE EXPRESSED IN RAT-BRAIN AND SPINAL-CORD DURING A SPECIFIC PERIOD OF NEURONAL DEVELOPMENT [J].
AKAGI, H ;
HIRAI, K ;
HISHINUMA, F .
FEBS LETTERS, 1991, 281 (1-2) :160-166
[3]   PROTEIN-KINASE INHIBITOR, H-7, DIRECTLY AFFECTS N-METHYL-D-ASPARTATE RECEPTOR CHANNELS [J].
AMADOR, M ;
DANI, JA .
NEUROSCIENCE LETTERS, 1991, 124 (02) :251-255
[4]  
ANGELOTTI TP, 1993, MOL PHARMACOL, V44, P1202
[5]  
ANGELOTTI TP, 1993, J NEUROSCI, V13, P1429
[6]   QUISQUALATE METABOTROPIC RECEPTORS MODULATE NMDA CURRENTS AND FACILITATE INDUCTION OF LONG-TERM POTENTIATION THROUGH PROTEIN-KINASE-C [J].
ANIKSZTEJN, L ;
OTANI, S ;
BENARI, Y .
EUROPEAN JOURNAL OF NEUROSCIENCE, 1992, 4 (06) :500-505
[7]   MODULATION OF VERTEBRATE NEURONAL CALCIUM CHANNELS BY TRANSMITTERS [J].
ANWYL, R .
BRAIN RESEARCH REVIEWS, 1991, 16 (03) :265-281
[8]   STIMULATION OF PROTEIN TYROSINE PHOSPHORYLATION BY NMDA RECEPTOR ACTIVATION [J].
BADING, H ;
GREENBERG, ME .
SCIENCE, 1991, 253 (5022) :912-914
[9]   MOLECULAR-BIOLOGY OF THE GABA-A RECEPTOR - THE RECEPTOR CHANNEL SUPERFAMILY [J].
BARNARD, EA ;
DARLISON, MG ;
SEEBURG, P .
TRENDS IN NEUROSCIENCES, 1987, 10 (12) :502-509
[10]   GAMMA-AMINOBUTYRIC ACIDA RECEPTOR HETEROGENEITY IS INCREASED BY ALTERNATIVE SPLICING OF A NOVEL BETA-SUBUNIT GENE TRANSCRIPT [J].
BATESON, AN ;
LASHAM, A ;
DARLISON, MG .
JOURNAL OF NEUROCHEMISTRY, 1991, 56 (04) :1437-1440