Molecular organization of the postsynaptic specialization

被引:268
作者
Sheng, M
机构
[1] Massachusetts Gen Hosp, Dept Neurobiol, Boston, MA 02114 USA
[2] Massachusetts Gen Hosp, Howard Hughes Med Inst, Boston, MA 02114 USA
[3] Harvard Univ, Sch Med, Boston, MA 02114 USA
关键词
D O I
10.1073/pnas.111146298
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
A specific set of molecules including glutamate receptors is targeted to the postsynaptic specialization of excitatory synapses in the brain, gathering in a structure known as the postsynaptic density (PSD). Synaptic targeting of glutamate receptors depends on interactions between the C-terminal tails of receptor subunits and specific: PDZ domain-containing scaffold proteins in the PSD. These scaffold proteins assemble a specialized protein complex around each class of glutamate receptor that functions in signal transduction, cytoskeletal anchoring, and trafficking of the receptors. Among the glutamate receptor subtypes. the N-methyl-D-aspartate receptor is relatively stably integrated in the PSD, whereas the alpha -amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor moves in and out of the postsynaptic membrane in highly dynamic fashion. The distinctive cell biological behaviors of N-methyl-D-aspartate a nd alpha -amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors can be explained by their differential interactions with cytoplasmic proteins.
引用
收藏
页码:7058 / 7061
页数:4
相关论文
共 71 条
[31]   LTP mechanisms: from silence to four-lane traffic [J].
Malinow, R ;
Mainen, ZF ;
Hayashi, Y .
CURRENT OPINION IN NEUROBIOLOGY, 2000, 10 (03) :352-357
[32]   Regulation of AMPA receptor-mediated synaptic transmission by clathrin-dependent receptor internalization [J].
Man, HY ;
Lin, JW ;
Ju, WH ;
Ahmadian, G ;
Liu, LD ;
Becker, LE ;
Sheng, M ;
Wang, YT .
NEURON, 2000, 25 (03) :649-662
[33]   Phosphorylation of serine-880 in GluR2 by protein kinase C prevents its C terminus from binding with glutamate receptor-interacting protein [J].
Matsuda, S ;
Mikawa, S ;
Hirai, H .
JOURNAL OF NEUROCHEMISTRY, 1999, 73 (04) :1765-1768
[34]   Disruption of AMPA receptor GluR2 clusters following long-term depression induction in cerebellar Purkinje neurons [J].
Matsuda, S ;
Launey, T ;
Mikawa, S ;
Hirai, H .
EMBO JOURNAL, 2000, 19 (12) :2765-2774
[35]   Enhanced long-term potentiation and impaired learning in mice with mutant postsynaptic density-95 protein [J].
Migaud, M ;
Charlesworth, P ;
Dempster, M ;
Webster, LC ;
Watabe, AM ;
Makhinson, M ;
He, Y ;
Ramsay, MF ;
Morris, RGM ;
Morrison, JH ;
O'Dell, TJ ;
Grant, SGN .
NATURE, 1998, 396 (6710) :433-439
[36]   Role of the carboxy-terminal region of the GluRε2 subunit in synaptic localization of the NMDA receptor channel [J].
Mori, H ;
Manabe, T ;
Watanabe, M ;
Satoh, Y ;
Suzuki, N ;
Toki, S ;
Nakamura, K ;
Yagi, T ;
Kushiya, E ;
Takahashi, T ;
Inoue, Y ;
Sakimura, K ;
Mishina, M .
NEURON, 1998, 21 (03) :571-580
[37]  
Naisbitt S, 1997, J NEUROSCI, V17, P5687
[38]   Shank, a novel family of postsynaptic density proteins that binds to the NMDA receptor/PSD-95/GKAP complex and cortactin [J].
Naisbitt, S ;
Kim, E ;
Tu, JC ;
Xiao, B ;
Sala, C ;
Valtschanoff, J ;
Weinberg, RJ ;
Worley, PF ;
Sheng, M .
NEURON, 1999, 23 (03) :569-582
[39]  
Niethammer M, 1996, J NEUROSCI, V16, P2157
[40]   NSF binding to GluR2 regulates synaptic transmission [J].
Nishimune, A ;
Isaac, JTR ;
Molnar, E ;
Noel, J ;
Nash, SR ;
Tagaya, M ;
Collingridge, GL ;
Nakanishi, S ;
Henley, JM .
NEURON, 1998, 21 (01) :87-97