Structural investigation of Nucleophosmin interaction with the tumor suppressor Fbw7γ (398 views)
Oncogenesis (ISSN: 2157-9024), 2017; 6(9): N/D-N/D.
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Paper type: Journal Article,
Impact factor: 4.722, 5-year impact factor: 4.692
Url: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85032725431&doi=10.1038%2foncsis.2017.78&partnerID=40&md5=75a2dbef3e5944b1ef2c7a26491ee922
Keywords: Centromere Protein W, F Box Wd Repeat Containing Protein 7, F Box Wd Repeat Containing Protein 7 Gamma, Human Immunodeficiency Virus Protein, Nuclear Protein, Nucleophosmin, Transactivator Protein, Tumor Suppressor Protein, Unclassified Drug, Amino Terminal Sequence, Article, Carboxy Terminal Sequence, Controlled Study, Molecular Docking, Molecular Dynamics, Nucleolar Localization Signal, Priority Journal, Protein Domain, Protein Expression, Protein Protein Interaction, Protein Structure, Site Directed Mutagenesis, Structural Model,
Affiliations:
*** IBB - CNR ***
Istituto di Biologia e Patologia Molecolari, Consiglio Nazionale delle Ricerche, Roma, Italy
Dipartimento di Scienze Mediche, Orali e Biotecnologiche, Università di Chieti-Pescara G d'Annunzio, Via dei Vestini 31, Chieti, 66100, Italy
CeSI-Met, Università di Chieti-Pescara G d'Annunzio, Chieti, Italy
Dipartimento di Biologia e Biotecnologie C Darwin, Sapienza Università di Roma, Roma, Italy
CINECA Consorzio Interuniversitario, Sede di Roma, Roma, Italy
Dipartimento di Farmacia, Università di Napoli Federico II, Napoli, Italy
Istituto di Biostrutture e Bioimmagini, Consiglio Nazionale delle Ricerche, Napoli, Italy
References:
Not available.
Oncogenesis (ISSN: 2157-9024), 2017; 6(9): N/D-N/D.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 4.722, 5-year impact factor: 4.692
Url: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85032725431&doi=10.1038%2foncsis.2017.78&partnerID=40&md5=75a2dbef3e5944b1ef2c7a26491ee922
Keywords: Centromere Protein W, F Box Wd Repeat Containing Protein 7, F Box Wd Repeat Containing Protein 7 Gamma, Human Immunodeficiency Virus Protein, Nuclear Protein, Nucleophosmin, Transactivator Protein, Tumor Suppressor Protein, Unclassified Drug, Amino Terminal Sequence, Article, Carboxy Terminal Sequence, Controlled Study, Molecular Docking, Molecular Dynamics, Nucleolar Localization Signal, Priority Journal, Protein Domain, Protein Expression, Protein Protein Interaction, Protein Structure, Site Directed Mutagenesis, Structural Model,
Affiliations:
*** IBB - CNR ***
Istituto di Biologia e Patologia Molecolari, Consiglio Nazionale delle Ricerche, Roma, Italy
Dipartimento di Scienze Mediche, Orali e Biotecnologiche, Università di Chieti-Pescara G d'Annunzio, Via dei Vestini 31, Chieti, 66100, Italy
CeSI-Met, Università di Chieti-Pescara G d'Annunzio, Chieti, Italy
Dipartimento di Biologia e Biotecnologie C Darwin, Sapienza Università di Roma, Roma, Italy
CINECA Consorzio Interuniversitario, Sede di Roma, Roma, Italy
Dipartimento di Farmacia, Università di Napoli Federico II, Napoli, Italy
Istituto di Biostrutture e Bioimmagini, Consiglio Nazionale delle Ricerche, Napoli, Italy
References:
Not available.
Structural investigation of Nucleophosmin interaction with the tumor suppressor Fbw7γ
Nucleophosmin (NPM1) is a multifunctional nucleolar protein implicated in ribogenesis, centrosome duplication, cell cycle control, regulation of DNA repair and apoptotic response to stress stimuli. The majority of these functions are played through the interactions with a variety of protein partners. NPM1 is frequently overexpressed in solid tumors of different histological origin. Furthermore NPM1 is the most frequently mutated protein in acute myeloid leukemia (AML) patients. Mutations map to the C-terminal domain and lead to the aberrant and stable localization of the protein in the cytoplasm of leukemic blasts. Among NPM1 protein partners, a pivotal role is played by the tumor suppressor Fbw7γ, an E3-ubiquitin ligase that degrades oncoproteins like c-MYC, cyclin E, Notch and c-jun. In AML with NPM1 mutations, Fbw7γ is degraded following its abnormal cytosolic delocalization by mutated NPM1. This mechanism also applies to other tumor suppressors and it has been suggested that it may play a key role in leukemogenesis. Here we analyse the interaction between NPM1 and Fbw7γ, by identifying the protein surfaces implicated in recognition and key aminoacids involved. Based on the results of computational methods, we propose a structural model for the interaction, which is substantiated by experimental findings on several site-directed mutants. We also extend the analysis to two other NPM1 partners (HIV Tat and CENP-W) and conclude that NPM1 uses the same molecular surface as a platform for recognizing different protein partners. We suggest that this region of NPM1 may be targeted for cancer treatment. © The Author(s) 2017.
Nucleophosmin (NPM1) is a multifunctional nucleolar protein implicated in ribogenesis, centrosome duplication, cell cycle control, regulation of DNA repair and apoptotic response to stress stimuli. The majority of these functions are played through the interactions with a variety of protein partners. NPM1 is frequently overexpressed in solid tumors of different histological origin. Furthermore NPM1 is the most frequently mutated protein in acute myeloid leukemia (AML) patients. Mutations map to the C-terminal domain and lead to the aberrant and stable localization of the protein in the cytoplasm of leukemic blasts. Among NPM1 protein partners, a pivotal role is played by the tumor suppressor Fbw7γ, an E3-ubiquitin ligase that degrades oncoproteins like c-MYC, cyclin E, Notch and c-jun. In AML with NPM1 mutations, Fbw7γ is degraded following its abnormal cytosolic delocalization by mutated NPM1. This mechanism also applies to other tumor suppressors and it has been suggested that it may play a key role in leukemogenesis. Here we analyse the interaction between NPM1 and Fbw7γ, by identifying the protein surfaces implicated in recognition and key aminoacids involved. Based on the results of computational methods, we propose a structural model for the interaction, which is substantiated by experimental findings on several site-directed mutants. We also extend the analysis to two other NPM1 partners (HIV Tat and CENP-W) and conclude that NPM1 uses the same molecular surface as a platform for recognizing different protein partners. We suggest that this region of NPM1 may be targeted for cancer treatment. © The Author(s) 2017.
Structural investigation of Nucleophosmin interaction with the tumor suppressor Fbw7γ
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Structural investigation of Nucleophosmin interaction with the tumor suppressor Fbw7γ
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View Export to BibTeX Export to EndNote
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Impact Factor: 4.779
View Export to BibTeX Export to EndNote
Lirussi L, Antoniali G, Vascotto C, D'Ambrosio C, Poletto M, Romanello M, Marasco D, Leone M, Quadrifoglio F, Bhakat KK, Scaloni A, Tell G
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Mol Biol Cell (ISSN: 1059-1524), 2012 Oct 15; 23(20): 4079-4096.
Impact Factor: 4.803
View Export to BibTeX Export to EndNote
Tagliamonte M, Marasco D, Ruggiero A, de Stradis A, Tornesello ML, Totrov M, Buonaguro FM, Buonaguro L
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Impact Factor: 3.73
View Export to BibTeX Export to EndNote
Vitagliano L, Fiume G, Scognamiglio PL, Doti N, Cannavo R, Puca A, Pedone C, Scala G, Quinto I, Marasco D
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Biochimie (ISSN: 0300-9084, 1638-6183, 1638-6183electronic), 2011 Sep; 93(9): 1592-1600.
Impact Factor: 3.022
View Export to BibTeX Export to EndNote
Salvatore E, Di Maio L, Filla A, Ferrara AM, Rinaldi C, Sacca F, Peluso S, Macchia PE, Pappata S, De Michele G
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Impact Factor: 4.48
View Export to BibTeX Export to EndNote
Autiero I, Costantini S, Colonna G
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Plos One (ISSN: 1932-6203linking), 2008 Oct 8; 4 (10 ): e7350-N/D.
Impact Factor:
View Export to BibTeX Export to EndNote
Malaguarnera R, Vella V, Pandini G, Sanfilippo M, Pezzino V, Vigneri R, Frasca F
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Impact Factor: 4.533
View Export to BibTeX Export to EndNote
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Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2007 Jan 12; 282(2): 831-835.
Impact Factor: 5.581
View Export to BibTeX Export to EndNote
Santelli E, Leone M, Li C, Fukushima T, Preece NE, Olson AJ, Ely KR, Reed JC, Pellecchia M, Liddington RC, Matsuzawa S-I
* Structural analysis of Siah1-Siah-interacting protein interactions and insights into the assembly of an E3 ligase multiprotein complex (833 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 Oct 7; 280(40): 34278-34287.
Impact Factor: 5.854
View Export to BibTeX Export to EndNote
Criscuolo C, Mancini P, Menchise V, Sacca F, De Michele G, Banfi S, Filla A
* Very late onset in ataxia oculomotor apraxia type I [1] (362 views)
Ann Neurol (ISSN: 0364-5134), 2005 May; 57(5): 777-777.
Impact Factor: 7.571
View Export to BibTeX Export to EndNote
Saviano M, Isernia C, Bassarello C, Di Lello P, Galdiero S, Mierke DF, Benedetti E, Pedone C
* Conformational analysis by NMR and distance geometry techniques of a peptide mimetic of the third helix of the Antennapedia homeodomain (566 views)
J Pept Res (ISSN: 1397-002x), 2005 Feb; 65(2): 200-208.
Impact Factor: 1.741
View Export to BibTeX Export to EndNote
Borgatti M, Lampronti I, Romanelli A, Pedone C, Saviano M, Bianchi N, Mischiati C, Gambari R
* Transcription factor decoy molecules based on a peptide nucleic acid (PNA)-DNA chimera mimicking Sp1 binding sites (915 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2003 Feb 28; 278(9): 7500-7509.
Impact Factor: 6.482
View Export to BibTeX Export to EndNote
17 Records (15 excluding Abstracts).
Total impact factor: 92.609 (81.308 excluding Abstracts).
Total 5 year impact factor: 99.363 (83.766 excluding Abstracts).
Total impact factor: 92.609 (81.308 excluding Abstracts).
Total 5 year impact factor: 99.363 (83.766 excluding Abstracts).
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