Towards the Phosphoproteome of Trypanosomatids
The identification and localization of protein phosphorylation sites provide clues to what proteins or pathways might be activated in a given condition, helping to improve our understanding about signaling networks. Advances in strategies for enrichment o
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Towards the Phosphoproteome of Trypanosomatids Fabricio K. Marchini, Lyris Martins Franco de Godoy, Michel Batista, Fernanda G. Kugeratski, and Marco A. Krieger
Abstract The identification and localization of protein phosphorylation sites provide clues to what proteins or pathways might be activated in a given condition, helping to improve our understanding about signaling networks. Advances in strategies for enrichment of phosphorylated peptides/proteins, mass spectrometry (MS) instrumentation, and specific MS techniques for identification and quantification of post-translational modifications have allowed for large-scale mapping of phosphorylation sites, promoting the field of phosphoproteomics. The great promise of phosphoproteomics is to unravel the dynamics of signaling networks, a layer of the emerging field of systems biology. Until a few years ago only a small number of phosphorylation sites had been described. Following large-scale trends, recent phosphoproteomic studies have reported the mapping of thousands of phosphorylation sites in trypanosomatids. However, quantitative information about the regulation of such sites in different conditions is still lacking. In this chapter, we provide a historical overview of phosphoproteomic studies for trypanosomatids and discuss some challenges and perspectives in the field.
Abbreviations 2D-DIGE 2DE AGC ALK aPK
Two dimensional differential gel electrophoresis Two dimensional electrophoresis Kinases containing PKA, PKG, and PKC Anaplastic lymphoma kinase Atypical protein kinase
F.K. Marchini • L.M.F. de Godoy • M. Batista F.G. Kugeratski • M.A. Krieger (*) Functional Genomics Laboratory, Fiocruz – Parana, Brazil e-mail: [email protected] A.L.S. Santos et al. (eds.), Proteins and Proteomics of Leishmania and Trypanosoma, Subcellular Biochemistry 74, DOI 10.1007/978-94-007-7305-9_15, © Springer Science+Business Media Dordrecht 2014
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CAMK CaMKK CDK1 CID CK CMGC
CRK DGF DHB DYRK ECD EGFR ePK ERK ERLIC ESI ETD FRAP GMD GSK3 HCD HILIC HOP HSP IDA IgE-HRF IMAC iTRAQ LC m/z MALDI MAP kinase MOAC mRNA MS MSA NEK NTA PEK Pf2αS PK PKA PP
F.K. Marchini et al.
Group of kinases containing calcium/calmodulin-dependent kinases Calmodulin-dependent protein kinase kinase Cyclin-dependent kinase 1 Collision-induced dissociation Casein-kinase Group of kinases containing cyclin-dependent kinases, mitogenactivated protein kinases, Glycogen synthase kinases, and CDK-like kinases. CT10 regulator of kinase Dispersed gene family 2,5-dihydroxybenzoic acid Dual-specificity tyrosine-regulated kinase Electron capture dissociation Epidermal growth factor receptor Eukaryotic protein kinase Extracellular signal-regulated kinase Electrostatic repulsion- hydrophilic interaction chromatography Electron spray ionization Electron transfer dissociation FKBP12-rapamycin-associated protein Glycosomal malate dehydrogenase Glycogen synthase kinase 3 Higher-energy C-trap dissociation Hydrophilic interaction chromatography HSP organizing protein Heat shock protein Iminodiacetic acid Immuno
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