Molecular basis of the PED/PEA15 interaction with the C-terminal fragment of phospholipase D1 revealed by NMR spectroscopy |
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| Authors: | Biancamaria Farina Nunzianna Doti Luciano Pirone Gaetano Malgieri Emilia M. Pedone Menotti Ruvo Roberto Fattorusso |
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| Affiliation: | 1. Istituto di Biostrutture e Bioimmagini, CNR, Napoli, Italy;2. Dipartimento di Scienze e Tecnologie Ambientali, Biologiche e Farmaceutiche, Seconda Università di Napoli, Caserta, Italy |
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| Abstract: | PED/PEA15 is a small protein involved in many protein–protein interactions that modulates the function of a number of key cellular effectors involved in major cell functions, including apoptosis, proliferation and glucose metabolism. In particular, PED/PEA15 interacts with the phospholipase D (PLD) isoforms 1 and 2 increasing protein kinase C-α isoform activity and affects both insulin-stimulated glucose transport and glucose-stimulated insulin secretion. |
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| Keywords: | PED/PEA15, Phosphoprotein Enriched in Diabetes/Phosphoprotein Enriched in Astrocytes 15 DED, death effector domain PLD1, phospholipase D1 PKC-α, protein kinase C-α isoform ERK, extracellular signal-regulated kinase HSQC, heteronuclear single quantum coherence CSP, chemical shift perturbation STD, saturation transfer difference SD, standard deviation TOCSY, total correlation spectroscopy NOESY, nuclear Overhauser effect spectroscopy ELISA, enzyme-linked immunosorbent assay MBP, Maltose Binding Protein |
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