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Metabolic control of Ca2+/calmodulin-dependent protein kinase II (CaMKII)-mediated caspase-2 suppression by the B55β/protein phosphatase 2A (PP2A).

Publication ,  Journal Article
Huang, B; Yang, C-S; Wojton, J; Huang, N-J; Chen, C; Soderblom, EJ; Zhang, L; Kornbluth, S
Published in: J Biol Chem
December 26, 2014

High levels of metabolic activity confer resistance to apoptosis. Caspase-2, an apoptotic initiator, can be suppressed by high levels of nutrient flux through the pentose phosphate pathway. This metabolic control is exerted via inhibitory phosphorylation of the caspase-2 prodomain by activated Ca(2+)/calmodulin-dependent protein kinase II (CaMKII). We show here that this activation of CaMKII depends, in part, on dephosphorylation of CaMKII at novel sites (Thr(393)/Ser(395)) and that this is mediated by metabolic activation of protein phosphatase 2A in complex with the B55β targeting subunit. This represents a novel locus of CaMKII control and also provides a mechanism contributing to metabolic control of apoptosis. These findings may have implications for metabolic control of the many CaMKII-controlled and protein phosphatase 2A-regulated physiological processes, because both enzymes appear to be responsive to alterations in glucose metabolized via the pentose phosphate pathway.

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Published In

J Biol Chem

DOI

EISSN

1083-351X

Publication Date

December 26, 2014

Volume

289

Issue

52

Start / End Page

35882 / 35890

Location

United States

Related Subject Headings

  • Xenopus laevis
  • Xenopus Proteins
  • Protein Processing, Post-Translational
  • Protein Phosphatase 2
  • Protein Binding
  • Phosphorylation
  • Humans
  • HEK293 Cells
  • Glucose-6-Phosphate
  • Enzyme Activation
 

Citation

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Huang, B., Yang, C.-S., Wojton, J., Huang, N.-J., Chen, C., Soderblom, E. J., … Kornbluth, S. (2014). Metabolic control of Ca2+/calmodulin-dependent protein kinase II (CaMKII)-mediated caspase-2 suppression by the B55β/protein phosphatase 2A (PP2A). J Biol Chem, 289(52), 35882–35890. https://doi.org/10.1074/jbc.M114.585844
Huang, Bofu, Chih-Sheng Yang, Jeffrey Wojton, Nai-Jia Huang, Chen Chen, Erik J. Soderblom, Liguo Zhang, and Sally Kornbluth. “Metabolic control of Ca2+/calmodulin-dependent protein kinase II (CaMKII)-mediated caspase-2 suppression by the B55β/protein phosphatase 2A (PP2A).J Biol Chem 289, no. 52 (December 26, 2014): 35882–90. https://doi.org/10.1074/jbc.M114.585844.
Huang B, Yang C-S, Wojton J, Huang N-J, Chen C, Soderblom EJ, et al. Metabolic control of Ca2+/calmodulin-dependent protein kinase II (CaMKII)-mediated caspase-2 suppression by the B55β/protein phosphatase 2A (PP2A). J Biol Chem. 2014 Dec 26;289(52):35882–90.
Huang, Bofu, et al. “Metabolic control of Ca2+/calmodulin-dependent protein kinase II (CaMKII)-mediated caspase-2 suppression by the B55β/protein phosphatase 2A (PP2A).J Biol Chem, vol. 289, no. 52, Dec. 2014, pp. 35882–90. Pubmed, doi:10.1074/jbc.M114.585844.
Huang B, Yang C-S, Wojton J, Huang N-J, Chen C, Soderblom EJ, Zhang L, Kornbluth S. Metabolic control of Ca2+/calmodulin-dependent protein kinase II (CaMKII)-mediated caspase-2 suppression by the B55β/protein phosphatase 2A (PP2A). J Biol Chem. 2014 Dec 26;289(52):35882–35890.

Published In

J Biol Chem

DOI

EISSN

1083-351X

Publication Date

December 26, 2014

Volume

289

Issue

52

Start / End Page

35882 / 35890

Location

United States

Related Subject Headings

  • Xenopus laevis
  • Xenopus Proteins
  • Protein Processing, Post-Translational
  • Protein Phosphatase 2
  • Protein Binding
  • Phosphorylation
  • Humans
  • HEK293 Cells
  • Glucose-6-Phosphate
  • Enzyme Activation