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Biochim Biophys Acta. 2011 Sep;1814(9):1134-9. doi: 10.1016/j.bbapap.2011.04.015. Epub 2011 May 5.

Identification of the phosphorylation sites in the survival motor neuron protein by protein kinase A.

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  • 1Department of Biological Sciences, University of Delaware, Newark, DE, USA. wcy@UDel.Edu


The survival motor neuron (SMN) protein plays an essential role in the assembly of uridine-rich small nuclear ribonuclear protein complexes. Phosphorylation of SMN can regulate its function, stability, and sub-cellular localization. This study shows that protein kinase A (PKA) phosphorylates SMN both in vitro and in vivo. Bioinformatic analysis predicts 12 potential PKA phosphorylation sites in human SMN. Mass spectrometric analysis of a tryptic digest of SMN after PKA phosphorylation identified five distinct phosphorylation sites in SMN (serines 4, 5, 8, 187 and threonine 85). Mutagenesis of this subset of PKA-phosphorylated sites in SMN affects association of SMN with Gemin2 and Gemin8. This result indicates that phosphorylation of SMN by PKA may play a role in regulation of the in vivo function of SMN.

Copyright © 2011 Elsevier B.V. All rights reserved.

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