Mediation by calcium/calmodulin-dependent protein kinase II of suppression of GABAA receptors by NMDA

2000 ◽  
Vol 43 (6) ◽  
pp. 655-662 ◽  
Author(s):  
Dianshi Wang ◽  
Hui Lü ◽  
Tianle Xu
1998 ◽  
Vol 67 (2) ◽  
pp. 145-152 ◽  
Author(s):  
Wendy W. Waters ◽  
Pat L. Chen ◽  
Newell H. McArthur ◽  
Pete A. Moreno ◽  
Paul G. Harms

2014 ◽  
Vol 106 (2) ◽  
pp. 679a
Author(s):  
Pabak Sarkar ◽  
Kaitlin Davis ◽  
Henry L. Puhl ◽  
Jithesh V. Veetil ◽  
Tuan A. Nguyen ◽  
...  

2012 ◽  
Vol 52 (2) ◽  
pp. 51-60 ◽  
Author(s):  
Stavroula Boubali ◽  
Kassiani Liopeta ◽  
Laura Virgilio ◽  
George Thyphronitis ◽  
George Mavrothalassitis ◽  
...  

2017 ◽  
Vol 2017 ◽  
pp. 1-13 ◽  
Author(s):  
D. E. Johnson ◽  
A. Hudmon

Calcium/calmodulin-dependent protein kinase II (CaMKII) is highly concentrated in the brain where its activation by the Ca2+sensor CaM, multivalent structure, and complex autoregulatory features make it an ideal translator of Ca2+signals created by different patterns of neuronal activity. We provide direct evidence that graded levels of kinase activity and extent of T287(T286αisoform) autophosphorylation drive changes in catalytic output and substrate selectivity. The catalytic domains of CaMKII phosphorylate purified PSDs much more effectively when tethered together in the holoenzyme versus individual subunits. Using multisubstrate SPOT arrays, high-affinity substrates are preferentially phosphorylated with limited subunit activity per holoenzyme, whereas multiple subunits or maximal subunit activation is required for intermediate- and low-affinity, weak substrates, respectively. Using a monomeric form of CaMKII to control T287autophosphorylation, we demonstrate that increased Ca2+/CaM-dependent activity for all substrates tested, with the extent of weak, low-affinity substrate phosphorylation governed by the extent of T287autophosphorylation. Our data suggest T287autophosphorylation regulates substrate gating, an intrinsic property of the catalytic domain, which is amplified within the multivalent architecture of the CaMKII holoenzyme.


2008 ◽  
Vol 54 (2) ◽  
pp. 319-330 ◽  
Author(s):  
Pilar Sánchez-Blázquez ◽  
María Rodríguez-Muñoz ◽  
Carlos Montero ◽  
Elena de la Torre-Madrid ◽  
Javier Garzón

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