Regulatory phosphorylation of AMPA-type glutamate receptors by CaM-KII during long-term potentiation. Export

@article{citeulike:1019528, abstract = {Long-term potentiation (LTP), a cellular model of learning and memory, requires calcium-dependent protein kinases. Induction of LTP increased the phosphorus-32 labeling of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA)-type glutamate receptors (AMPA-Rs), which mediate rapid excitatory synaptic transmission. This AMPA-R phosphorylation appeared to be catalyzed by Ca2+- and calmodulin-dependent protein kinase II (CaM-KII): (i) it correlated with the activation and autophosphorylation of CaM-KII, (ii) it was blocked by the CaM-KII inhibitor KN-62, and (iii) its phosphorus-32 peptide map was the same as that of GluR1 coexpressed with activated CaM-KII in HEK-293 cells. This covalent modulation of AMPA-Rs in LTP provides a postsynaptic molecular mechanism for synaptic plasticity.}, address = {Vollum Institute, Oregon Health Sciences University, Portland, OR 97201, USA.}, author = {Barria, A. and Muller, D. and Derkach, V. and Griffith, L. C. and Soderling, T. R.}, citeulike-article-id = {1019528}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/9197267}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=9197267}, day = {27}, issn = {0036-8075}, journal = {Science}, keywords = {ampar\_p, ca1, camkii, kt}, month = {June}, number = {5321}, pages = {2042--2045}, posted-at = {2006-12-30 03:31:20}, priority = {2}, title = {Regulatory phosphorylation of AMPA-type glutamate receptors by CaM-KII during long-term potentiation.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/9197267}, volume = {276}, year = {1997} }

TY - JOUR ID - citeulike:1019528 L3 - citeulike-article-id:1019528 N2 - Long-term potentiation (LTP), a cellular model of learning and memory, requires calcium-dependent protein kinases. Induction of LTP increased the phosphorus-32 labeling of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA)-type glutamate receptors (AMPA-Rs), which mediate rapid excitatory synaptic transmission. This AMPA-R phosphorylation appeared to be catalyzed by Ca2+- and calmodulin-dependent protein kinase II (CaM-KII): (i) it correlated with the activation and autophosphorylation of CaM-KII, (ii) it was blocked by the CaM-KII inhibitor KN-62, and (iii) its phosphorus-32 peptide map was the same as that of GluR1 coexpressed with activated CaM-KII in HEK-293 cells. This covalent modulation of AMPA-Rs in LTP provides a postsynaptic molecular mechanism for synaptic plasticity. IS - 5321 JF - Science SN - 0036-8075 AD - Vollum Institute, Oregon Health Sciences University, Portland, OR 97201, USA. EP - 2045 TI - Regulatory phosphorylation of AMPA-type glutamate receptors by CaM-KII during long-term potentiation. VL - 276 SP - 2042 KW - ampar_p KW - ca1 KW - camkii KW - kt AU - Barria, A AU - Muller, D AU - Derkach, V AU - Griffith, LC AU - Soderling, TR PY - 1997/06/27/ UR - http://view.ncbi.nlm.nih.gov/pubmed/9197267 ER -