CaMK4 phosphorylates CREB1

Stable Identifier
Reaction [transition]
Homo sapiens
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The cAMP-responsive element binding protein (CREB), a key regulator of gene expression, is activated by phosphorylation on Ser-133. Several different protein kinases possess the capability of driving this phosphorylation, making it a point of convergence for multiple intracellular signaling cascades. Work in neurons has indicated that physiologic synaptic stimulation recruits a fast calmodulin kinase IV (CaMKIV)-dependent pathway that dominates early signaling to CREB. Activated CaMKIV (CAMK4) phosphorylates CREB1 at S133, thereby initiating the transcription of CREB1-regulated set of genes, leading to protein synthesis and long lasting changes that underlie synaptic plasticity.

Literature References
PubMed ID Title Journal Year
19001277 Loss of the Ca2+/calmodulin-dependent protein kinase type IV in dopaminoceptive neurons enhances behavioral effects of cocaine

Schumann, G, Klugmann, M, Guindalini, C, de Fonseca, FR, Perreau-Lenz, S, Sch├╝tz, G, Vallada, H, Westphal, M, Parkitna, JR, Konopka, W, Sanchis-Segura, C, Schneider, M, Breen, G, Desrivieres, S, Engblom, D, Spanagel, R, Laranjeira, R, Bilbao, A

Proc Natl Acad Sci U S A 2008
Catalyst Activity

calmodulin-dependent protein kinase activity of p-S12.S13,T200-CAMK4:CALM1:4xCa2+ [nucleoplasm]

Inferred From
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