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Phosphoproteomic identification and functional characterization of protein kinase substrates by 2D-DIGE and Phos-tag PAGE
- Source :
- Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1867:57-61
- Publication Year :
- 2019
- Publisher :
- Elsevier BV, 2019.
-
Abstract
- Protein phosphorylation is one of the most common post-translational modifications in eukaryotes and can regulate diverse properties of proteins. Protein kinases are encoded by more than 500 genes in higher eukaryotes and play central roles in various cellular signaling pathways. Consequently, genetic abnormalities of protein kinases have been implicated in many diseases. To fully understand the complex phosphorylation-mediated signaling networks, it is important to globally identify and functionally characterize in vivo substrates of individual protein kinases. Advances in electrophoresis-based phosphoproteomic technologies such as two-dimensional difference gel electrophoresis (2D-DIGE) following immobilized metal affinity chromatography (IMAC) and phosphate-affinity Phos-tag PAGE have enabled efficient and detailed analysis of protein kinase substrates. Here, we describe physiological functions of the newly identified substrates of several disease-related protein kinases including ERK, PKD and PINK1.
- Subjects :
- Proteomics
0301 basic medicine
MAPK/ERK pathway
Cell signaling
Difference gel electrophoresis
Biophysics
Biochemistry
Chromatography, Affinity
Analytical Chemistry
Two-Dimensional Difference Gel Electrophoresis
03 medical and health sciences
0302 clinical medicine
Tandem Mass Spectrometry
Animals
Humans
Protein phosphorylation
Phosphorylation
Protein kinase A
Molecular Biology
Kinase
Chemistry
Phosphoproteomics
Phosphoproteins
030104 developmental biology
030220 oncology & carcinogenesis
Protein Kinases
Protein Processing, Post-Translational
Signal Transduction
Subjects
Details
- ISSN :
- 15709639
- Volume :
- 1867
- Database :
- OpenAIRE
- Journal :
- Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- Accession number :
- edsair.doi.dedup.....876750d783a906c6afc7fc9682420e8f