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J Biol Chem. 2012 Nov 16;287(47):39361-8. doi: 10.1074/jbc.M112.366617. Epub 2012 Oct 1.

Regulatory subunit myristoylation antagonizes calcineurin phosphatase activation in yeast.

Author information

  • 1Department of Physiology, Program in Oncology, Marlene and Stewart Greenbaum Cancer Center, the University of Maryland Baltimore School of Medicine, Baltimore, Maryland 21201, USA.

Abstract

The Ca(2+)/calmodulin-stimulated protein phosphatase calcineurin is a critical component of Ca(2+) signaling cascades in eukaryotic cells. Myristoylation of the regulatory subunit of calcineurin (CNB) is conserved from yeast to humans. Here, we show that CNB myristoylation antagonizes phosphatase activation in yeast. Disruption of CNB myristoylation by mutation of the myristoylated glycine triggered constitutive expression of a calcineurin-dependent reporter gene and enhanced calcineurin-dependent phenotypes. Basal phosphatase activity was also increased in nmt1-181 yeast with reduced N-myristoyltransferase activity. Our findings are the first demonstration of a functional role for CNB myristoylation and reveal the importance of Nmt1 in modulating cellular calcineurin activation.

PMID:
23027860
[PubMed - indexed for MEDLINE]
PMCID:
PMC3501033
Free PMC Article

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