Threonine 89 Is an Important Residue of Profilin-1 That Is Phosphorylatable by Protein Kinase A

Dynamic regulation of actin cytoskeleton is at the heart of all actin-based cellular events. In this study, we sought to identify novel post-translational modifications of Profilin-1 (Pfn1), an important regulator of actin polymerization in cells. We performed in vitro protein kinase assay followed...

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Veröffentlicht in:	PloS one 2016-05, Vol.11 (5), p.e0156313-e0156313
Hauptverfasser:	Gau, David, Veon, William, Zeng, Xuemei, Yates, Nathan, Shroff, Sanjeev G, Koes, David R, Roy, Partha
Format:	Artikel
Sprache:	eng
Schlagworte:	Actin Actin Cytoskeleton - metabolism Animals Binding proteins Bioengineering Biological activity Biology Biology and Life Sciences Cattle Cell adhesion & migration Chemical properties Cyclic AMP-Dependent Protein Kinases - metabolism Cytoskeleton Dimensional changes Electrophoresis Electrophoresis, Gel, Two-Dimensional Forskolin Gel electrophoresis Health aspects HEK293 Cells Humans In vitro methods and tests Kinases Ligands Mammalian cells Mammals Mass spectrometry Medicine and Health Sciences Mice Models, Molecular Molecular dynamics Molecular Dynamics Simulation Mutation Nitric oxide Penicillin Phosphorylation Physical Sciences Plasmids Polymerization Post-translation Profilin Profilins - chemistry Profilins - metabolism Protein Binding Protein Conformation Protein interaction Protein kinase A Protein kinases Protein Processing, Post-Translational Proteins Proteolysis Scientific imaging Sequestering Spectrometry Tandem Mass Spectrometry Threonine Threonine - chemistry Threonine - metabolism Two dimensional analysis
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