Identification of the phosphorylation sites in the survival motor neuron protein by protein kinase A.
Publication/Presentation Date
9-1-2011
Abstract
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.
Volume
1814
Issue
9
First Page
1134
Last Page
1139
ISSN
0006-3002
Published In/Presented At
Wu, C. Y., Curtis, A., Choi, Y. S., Maeda, M., Xu, M. J., Berg, A., Joneja, U., Mason, R. W., Lee, K. H., & Wang, W. (2011). Identification of the phosphorylation sites in the survival motor neuron protein by protein kinase A. Biochimica et biophysica acta, 1814(9), 1134–1139. https://doi.org/10.1016/j.bbapap.2011.04.015
Disciplines
Medicine and Health Sciences
PubMedID
21609790
Department(s)
Department of Pathology and Laboratory Medicine
Document Type
Article