RGD Reference Report - 14-3-3 Proteins directly regulate Ca(2+)/calmodulin-dependent protein kinase kinase alpha through phosphorylation-dependent multisite binding. - Rat Genome Database

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14-3-3 Proteins directly regulate Ca(2+)/calmodulin-dependent protein kinase kinase alpha through phosphorylation-dependent multisite binding.

Authors: Ichimura, T  Taoka, M  Hozumi, Y  Goto, K  Tokumitsu, H 
Citation: Ichimura T, etal., FEBS Lett. 2008 Mar 5;582(5):661-5. doi: 10.1016/j.febslet.2008.01.037. Epub 2008 Jan 31.
RGD ID: 11041071
Pubmed: PMID:18242179   (View Abstract at PubMed)
DOI: DOI:10.1016/j.febslet.2008.01.037   (Journal Full-text)

Ca(2+)/calmodulin-dependent protein kinase kinase alpha (CaMKKalpha) plays critical roles in the modulation of neuronal cell survival as well as many other cellular activities. Here we show that 14-3-3 proteins directly regulate CaMKKalpha when the enzyme is phosphorylated by protein kinase A on either Ser74 or Ser475. Mutational analysis revealed that these two serines are both functional: the CaMKKalpha mutant with a mutation at either of these residues, but not the double mutant, was inhibited significantly by 14-3-3. The mode of regulation described herein differs the recently described mode of 14-3-3 regulation of CaMKKalpha.

Objects referenced in this article
Gene Camkk1 calcium/calmodulin-dependent protein kinase kinase 1 Rattus norvegicus
Gene Ywhag tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, gamma Rattus norvegicus
Gene Ywhah tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, eta Rattus norvegicus

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