Fe65 is characterized as an adaptor precursor (APP) through its PID2 element, as well as with the other members of the APP protein family. With the serum- and glucocorticoid-induced kinase 1 (SGK1) substrate specificity information, we found that the putative site of phosphorylation in Fe65 by SGK1 is present on its Ser(566) residue in (560)CRVRFLSFLA(569)(X60469). Thus, we demonstrated that Fe65 and the fluorescein-labeled Fe65 peptide FITC-(560)CRVRFLSFLA(569) are phosphorylated in vitro by SGK1. Phosphorylation of the Ser(566) residue was also demonstrated using a Ser566 phospho-specific antibody. The phospho Fe65 was found mainly in the nucleus, while Fe65 S556A mutant was localized primarily to the cytoplasm. Therefore, these data suggest that SGK1 phosphorylates the Ser(566) residue of Fe65 and that this phosphorylation promotes the migration of Fe65 to the nucleus of the cell.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.5483/bmbrep.2008.41.1.041 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Phosphorylation of Specificity Protein 3 Is Critical for Activation of β4-Galactosyltransferase 3 Gene Promoter in SH-SY5Y Human Neuroblastoma Cell Line.
Biol Pharm Bull
April 2021
Laboratory of Glycobiology, Department of Bioengineering, Nagaoka University of Technology.
Elevated expression of β4-galactosyltransferase (β4GalT) 3 is correlated with poor clinical outcome of neuroblastoma patients. Our recent study has revealed that the transcription of the β4GalT3 gene is activated by Specificity protein (Sp) 3 in SH-SY5Y human neuroblastoma cell line. Here we report the biological significance of the Sp3 phosphorylation in the transcriptional activation of the β4GalT3 gene.
View Article and Find Full Text PDFMolecular cloning, expression and characterization of acylpeptide hydrolase in the silkworm, Bombyx mori.
Gene
April 2016
School of Life Sciences, Chongqing University, Chongqing 400044, China. Electronic address:
Acylpeptide hydrolase (APH) can catalyze the release of the N-terminal amino acid from acetylated peptides. There were many documented examples of this enzyme in various prokaryotic and eukaryotic organisms. However, knowledge about APH in insects still remains unknown.
View Article and Find Full Text PDFRegulation Fe65 localization to the nucleus by SGK1 phosphorylation of its Ser566 residue.
BMB Rep
January 2008
School of Science Education, Chungbuk National University, Cheongju, Korea.
Fe65 is characterized as an adaptor precursor (APP) through its PID2 element, as well as with the other members of the APP protein family. With the serum- and glucocorticoid-induced kinase 1 (SGK1) substrate specificity information, we found that the putative site of phosphorylation in Fe65 by SGK1 is present on its Ser(566) residue in (560)CRVRFLSFLA(569)(X60469). Thus, we demonstrated that Fe65 and the fluorescein-labeled Fe65 peptide FITC-(560)CRVRFLSFLA(569) are phosphorylated in vitro by SGK1.
View Article and Find Full Text PDFApoptosis-associated tyrosine kinase (AATYK) has differential Ca2+-dependent phosphorylation states in response to survival and apoptotic conditions in cerebellar granule cells.
J Biol Chem
October 2005
Laboratory for Molecular Neurogenesis, RIKEN Brain Science Institute, Wako, Saitama 351-0198, Japan.
In dissociated cultures of cerebellar granule cells, extracellular high potassium (HK) and low potassium (LK) concentrations control cell survival and apoptosis, respectively. Apoptosis-associated tyrosine kinase (AATYK) is up-regulated during the LK-induced apoptosis. Overexpression of wild-type AATYK, but not its kinase-deficient mutant, stimulates apoptosis in LK.
View Article and Find Full Text PDFGlycosylation sites flank phosphorylation sites on synapsin I: O-linked N-acetylglucosamine residues are localized within domains mediating synapsin I interactions.
J Neurochem
July 1999
Department of Biological Chemistry, School of Medicine, Johns Hopkins University, Baltimore, Maryland 21205-2185, USA.
Synapsin I is concentrated in nerve terminals, where it appears to anchor synaptic vesicles to the cytoskeleton and thereby ensures a steady supply of fusion-competent synaptic vesicles. Although phosphorylation-dependent binding of synapsin I to cytoskeletal elements and synaptic vesicles is well characterized, little is known about synapsin I's O-linked N-acetylglucosamine (O-GlcNAc) modifications. Here, we identified seven in vivo O-GlcNAcylation sites on synapsin I by analysis of HPLC-purified digests of rat brain synapsin I.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!