Identification of the phosphorylation sites in the survival motor neuron protein by protein kinase A.
Biochim Biophys Acta
; 1814(9): 1134-9, 2011 Sep.
Article
in En
| MEDLINE
| ID: mdl-21609790
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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Cyclic AMP-Dependent Protein Kinases
/
SMN Complex Proteins
Type of study:
Diagnostic_studies
Limits:
Humans
Language:
En
Journal:
Biochim Biophys Acta
Year:
2011
Type:
Article
Affiliation country:
United States