Molecular basis of the PED/PEA15 interaction with the C-terminal fragment of phospholipase D1 revealed by NMR spectroscopy (678 views)
Bba-Gen Subjects (ISSN: 1570-9639, 0006-3002, 0925-4439), 2013 Sep; 1834(8): 1572-1580.
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Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 3.191, 5-year impact factor: 3.282
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84879048177&partnerID=40&md5=512e21ff48bb8d4814830568aa75948a
Keywords: Chemical Shift Perturbation, Death Domain, Ped Pea15 Protein, Protein-Protein Interaction, D4 Alpha Protein, Phospholipase D1, Phosphoprotein, Phosphoprotein Enriched In Astrocyte 15, Phosphoprotein Enriched In Diabetes, Protein Kinase C Alpha, Synthetic Peptide, Unclassified Drug, Human, Peptide Fragment, Signal Peptide, Allosterism, Article, Binding Site, Controlled Study, Enzyme Activity, Enzyme Linked Immunosorbent Assay, Nuclear Magnetic Resonance Spectroscopy, Priority Journal, Protein Analysis, Protein Binding, Protein Expression, Protein Protein Interaction, Chemistry, Metabolism, Protein Conformation, Enzyme-Linked Immunosorbent Assay, Intracellular Signaling Peptides And Proteins, Intracellular Signaling Peptides And Proteins Chemistry Metabolism, Peptide Fragments Chemistry Metabolism, Phospholipase D Chemistry Metabolism, Phosphoproteins Chemistry Metabolism,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, CNR, Napoli, Italy
Dipartimento di Scienze e Tecnologie Ambientali, Biologiche e Farmaceutiche, Seconda Università di Napoli, via Vivaldi 43, 81100
References:
Not available.
Bba-Gen Subjects (ISSN: 1570-9639, 0006-3002, 0925-4439), 2013 Sep; 1834(8): 1572-1580.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 3.191, 5-year impact factor: 3.282
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84879048177&partnerID=40&md5=512e21ff48bb8d4814830568aa75948a
Keywords: Chemical Shift Perturbation, Death Domain, Ped Pea15 Protein, Protein-Protein Interaction, D4 Alpha Protein, Phospholipase D1, Phosphoprotein, Phosphoprotein Enriched In Astrocyte 15, Phosphoprotein Enriched In Diabetes, Protein Kinase C Alpha, Synthetic Peptide, Unclassified Drug, Human, Peptide Fragment, Signal Peptide, Allosterism, Article, Binding Site, Controlled Study, Enzyme Activity, Enzyme Linked Immunosorbent Assay, Nuclear Magnetic Resonance Spectroscopy, Priority Journal, Protein Analysis, Protein Binding, Protein Expression, Protein Protein Interaction, Chemistry, Metabolism, Protein Conformation, Enzyme-Linked Immunosorbent Assay, Intracellular Signaling Peptides And Proteins, Intracellular Signaling Peptides And Proteins Chemistry Metabolism, Peptide Fragments Chemistry Metabolism, Phospholipase D Chemistry Metabolism, Phosphoproteins Chemistry Metabolism,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, CNR, Napoli, Italy
Dipartimento di Scienze e Tecnologie Ambientali, Biologiche e Farmaceutiche, Seconda Università di Napoli, via Vivaldi 43, 81100
References:
Not available.
Molecular basis of the PED/PEA15 interaction with the C-terminal fragment of phospholipase D1 revealed by NMR spectroscopy
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-alpha isoform activity and affects both insulin-stimulated glucose transport and glucose-stimulated insulin secretion. The C-terminal portion (residues 712-1074) of PLD1, named D4, is still able to interact with PED/PEA15. In this study we characterized, by means of NMR spectroscopy, the molecular interaction of PED/PEA15 with D4 alpha, a smaller region of D4, encompassing residues 712-818, shown to have the same affinity for PED/PEA15 and to induce the same effects as D4 in PED/PEA15-overexpressing cells. Chemical shift perturbation (CSP) studies allowed to define D4 alpha binding site of PED/PEA15 and to identify a smaller region likely affected by an allosteric effect. Moreover, ELISA-like experiments showed that three 20-mer overlapping synthetic peptides, covering the 762-801 region of D4 alpha, strongly inhibit PED/PEA15-D4 alpha interaction through their binding to PED/PEA15 with K(D)s in low micromolar range. Finally, molecular details of the interaction of PED/PEA15 with one of the three peptides have been revealed by CSP and saturation transfer difference (STD) analyses. (C) 2013 Elsevier B.V. All rights reserved.
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-alpha isoform activity and affects both insulin-stimulated glucose transport and glucose-stimulated insulin secretion. The C-terminal portion (residues 712-1074) of PLD1, named D4, is still able to interact with PED/PEA15. In this study we characterized, by means of NMR spectroscopy, the molecular interaction of PED/PEA15 with D4 alpha, a smaller region of D4, encompassing residues 712-818, shown to have the same affinity for PED/PEA15 and to induce the same effects as D4 in PED/PEA15-overexpressing cells. Chemical shift perturbation (CSP) studies allowed to define D4 alpha binding site of PED/PEA15 and to identify a smaller region likely affected by an allosteric effect. Moreover, ELISA-like experiments showed that three 20-mer overlapping synthetic peptides, covering the 762-801 region of D4 alpha, strongly inhibit PED/PEA15-D4 alpha interaction through their binding to PED/PEA15 with K(D)s in low micromolar range. Finally, molecular details of the interaction of PED/PEA15 with one of the three peptides have been revealed by CSP and saturation transfer difference (STD) analyses. (C) 2013 Elsevier B.V. All rights reserved.
Molecular basis of the PED/PEA15 interaction with the C-terminal fragment of phospholipase D1 revealed by NMR spectroscopy
Molecular basis of the PED/PEA15 interaction with the C-terminal fragment of phospholipase D1 revealed by NMR spectroscopy
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Impact Factor:
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Mercurio FA, Di Natale C, Pirone L, Vincenzi M, Marasco D, De Luca S, Pedone EM, Leone M
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Impact Factor: 2.641
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Impact Factor: 3.469
View Export to BibTeX Export to EndNote
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Impact Factor: 1.427
View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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Impact Factor: 2.999
View Export to BibTeX Export to EndNote
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Impact Factor: 5.317
View Export to BibTeX Export to EndNote
Pirone L, Smaldone G, Esposito C, Balasco N, Petoukhov MV, Spilotros A, Svergun DI, Di Gaetano S, Vitagliano L, Pedone E
* Proteins involved in sleep homeostasis: Biophysical characterization of INC and its partners (485 views) (PDF 220 views)
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Impact Factor: 3.112
View Export to BibTeX Export to EndNote
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* Regulating levels of the neuromodulator d-serine in human brain: structural insight into pLG72 and d-amino acid oxidase interaction (440 views) (PDF 242 views)
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Impact Factor: 3.902
View Export to BibTeX Export to EndNote
Ruvo M, Doti N, Lorenzo V, Vitagliano L, Mascanzoni F
* The Interacting Domains of PREP1 and p160 are Endowed with a Remarkable Structural Stability (402 views)
Mol Biotechnol (ISSN: 1073-6085, 1559-0305electronic, 1073-6085linking), 2016 May; 58(5): 328-339.
Impact Factor: 1.634
View Export to BibTeX Export to EndNote
Bottini A, Wu B, Barile E, De SK, Leone M, Pellecchia M
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Impact Factor: 2.98
View Export to BibTeX Export to EndNote
Correale S, de Paola I, Morgillo CM, Federico A, Zaccaro L, Pallante P, Galeone A, Fusco A, Pedone E, Luque FJ, Catalanotti B
* Structural Model of the hUbA1-UbcH10 Quaternary Complex: In Silico and Experimental Analysis of the Protein-Protein Interactions between E1, E2 and Ubiquitin (735 views)
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View Export to BibTeX Export to EndNote
Balasco N, Pirone L, Smaldone G, Di Gaetano S, Esposito L, Pedone E, Vitagliano L
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Diana D, Smaldone G, De Antonellis P, Pirone L, Carotenuto M, Alonzi A, Di Gaetano S, Zollo M, Pedone E, Fattorusso R
* Mapping Functional Interaction Sites of Human Prune C-Terminal Domain by NMR Spectroscopy in Human Cell Lysates (516 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2013 Sep 9; 19(37): 12217-12220.
Impact Factor: 5.696
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Attanasio F, Convertino M, Magno A, Caflisch A, Corazza A, Haridas H, Esposito G, Cataldo S, Pignataro B, Milardi D, Rizzarelli E
* Carnosine Inhibits Abeta(42) Aggregation By Perturbing The H-Bond Network In And Around The Central Hydrophobic Cluster (1148 views)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2013 Mar 18; 14(5): 583-592.
Impact Factor: 3.06
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Grasso G, Spoto G
* Plasmonics for the study of metal ion-protein interactions (657 views)
Anal Bioanal Chem (ISSN: 1618-2642), 2013 Feb; 405(6): 1833-1843.
Impact Factor: 3.578
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Mercurio FA, Marasco D, Pirone L, Scognamiglio PL, Pedone E, Pellecchia M, Leone M
* Heterotypic Sam-Sam Association Between Odin-Sam1 And Arap3-Sam: Binding Affinity And Structural Insights (604 views)
Chembiochem (ISSN: 1439-4227, 1439-9422, 1439-7633), 2013 Jan 2; 14(1): 100-106.
Impact Factor: 2.92
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Poletto M, Vascotto C, Scognamiglio PL, Lirussi L, Marasco D, Tell G
* Role Of The Unstructured N-Terminal Domain Of The Human Apurinic/Apyrimidinic Endonuclease 1 (hape1) In The Modulation Of Its Interaction With Nucleic Acids And Nucleophosmin (npm1) (572 views)
Biochem J (ISSN: 0264-6021, 1470-8728electronic, 0264-6021linking), 2013; 452(3): 545-557.
Impact Factor: 4.779
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Mercurio FA, Marasco D, Pirone L, Pedone E, Pellecchia M, Leone M
* Solution Structure of the First Sam Domain of Odin and Binding Studies with the EphA2 Receptor (623 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2012 Mar 13; 51(10): 2136-2145.
Impact Factor: 3.377
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Viparelli F, Doti N, Sandomenico A, Marasco D, Dathan NA, Miele C, Beguinot F, Monti SM, Ruvo M
* GSM48878: CD8 IL2-D2 (488 views)
Gene Expression Omnibus, 2011 Dec 2; 59(2): 302-308.
Impact Factor: 2.082
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Ruvo M, Sandomenico A, Tudisco L, De Falco S
* Branched peptides for the modulation of protein-protein interactions: More arms are better than one? (635 views)
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2011 Jun; 18(16): 2429-2437.
Impact Factor: 4.859
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Correale S, Pirone L, Di Marcotullio L, De Smaele E, Greco A, Mazzà D, Moretti M, Alterio V, Vitagliano L, Di Gaetano S, Gulino A, Pedone E
* Molecular organization of the cullin E3 ligase adaptor KCTD11 (789 views)
Biochimie (ISSN: 0300-9084, 1638-6183, 1638-6183electronic), 2011 Apr; 93(4): 715-724.
Impact Factor: 3.022
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Farina B, Pirone L, Russo L, Viparelli F, Doti N, Pedone C, Pedone E, Fattorusso R
* NMR backbone dynamics studies of human PED/PEA-15 outline protein functional sites (950 views)
Febs J (ISSN: 1742-4658, 1742-464x, 1742-4658electronic), 2010 Oct; 277(20): 4229-4240.
Impact Factor: 3.129
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Sandomenico A, Monti SM, Sabatella M, De Capua A, Tornatore L, Doti N, Viparelli F, Dathan NA, Pedone C, Ruvo M, Marasco D
* Protein-protein interactions: a simple strategy to identify binding sites and peptide antagonists (808 views)
Chem Biol Drug Des (ISSN: 1747-0285, 1747-0277), 2009 May; 73(5): 483-493.
Impact Factor: 2.473
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Vitagliano L, Ruggiero A, Pedone C, Berisio R
* Molecular dynamics studies of the P pilus rod subunit PapA (804 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2009 Mar; 15(3): 192-199.
Impact Factor: 1.807
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Merlino A, Varriale S, Coscia MR, Mazzarella L, Oreste U
* Structure and dimerization of the teleost transmembrane immunoglobulin region (600 views)
Journal Of Molecular Graphics & Modelling (ISSN: 1093-3263), 2008 Oct; 27(3): 401-407.
Impact Factor: 2.347
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Vitagliano L, Ruggiero A, Pedone C, Berisio R
* Conformational states and association mechanism of Yersinia pestis Caf1 subunits (576 views)
Biochem Biophys Res Commun (ISSN: 0006-291x, 1090-2104, 1090-2104electronic), 2008 Sep 8; 372(4): 804-810.
Impact Factor: 2.648
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Ruvo M, Marasco D, Viparelli F, Tornatore L, Sandomenico A, Doti N, Pedone C, Benedetti E, Monti SM
* Peptide antagonists of protein-protein interactions identified by screening protein fragments derived by enzyme degradation (458 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2008 Sep; 14(8): N/D-N/D.
Impact Factor: 1.654
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Viparelli F, Doti N, Sandomenico A, Marasco D, Dathan NA, Miele C, Beguinot F, Monti SM, Ruvo M
* Expression and purification of the D4 region of PLD1 and characterization of its interaction with PED-PEA15 (598 views)
Protein Expr Purif (ISSN: 1046-5928), 2008 Jun; 59(2): 302-308.
Impact Factor: 1.621
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Tornatore L, Marasco D, Dathan N, Vitale RM, Benedetti E, Papa S, Franzoso G, Ruvo M, Monti SM
* Gadd45 beta forms a homodimeric complex that binds tightly to MKK7 (918 views)
J Mol Biol (ISSN: 0022-2836, 0022-2283, 1089-8638), 2008 Apr 18; 378(1): 97-111.
Impact Factor: 5.673
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Vitagliano L, Ruggiero A, Pedone C, Berisio R
* A Molecular Dynamics Study of Pilus Subunits: Insights into Pilus Biogenesis (617 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2007 Apr 6; 367(4): 935-941.
Impact Factor: 4.472
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34 Records (31 excluding Abstracts).
Total impact factor: 107.753 (97.192 excluding Abstracts).
Total 5 year impact factor: 120.472 (110.255 excluding Abstracts).
Total impact factor: 107.753 (97.192 excluding Abstracts).
Total 5 year impact factor: 120.472 (110.255 excluding Abstracts).
678 views. Last view on Sunday 08 December 2024, 0:57:37
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