Journal
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
Volume 1814, Issue 9, Pages 1134-1139Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2011.04.015
Keywords
Spinal muscular atrophy; Survival motor neuron protein; Protein kinase A; Phosphorylation site
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Funding
- Nemours
- National Institutes of Health [2P20 RR016472-10, 5P20 RR020173-04]
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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 PICA 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 PICA may play a role in regulation of the in vivo function of SMN. (C) 2011 Elsevier B.V. All rights reserved.
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