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Aurelio Pio Nardozza
describes for SIIC the most significant aspects of his article
describe para SIIC los aspectos relevantes de su artículo


REACTIVE OXYGEN SPECIES CONTROL SHP-2 DIMERIZATION AND ACTIVITY

SHP-2 dimerization is stabilized by the formation of disulfide bonds and it is modulated by growth factors and by the cellular redox state. Notably, the dimeric form is less active compared to its the monomeric self-inhibited counterpart pointing to dimerization as an additional mechanism to control SHP-2 activity.

The article was published by
El artículo fue publicado por
Molecular and Cellular Biology
Volume / Volumen: 32
Number / Número: 10
First and last pages / Páginas inicial-final: 1998-2009
Year / Año: 2012
Month / Mes: may


This journal, which is covered by SIIC Data Bases,
is part of the bibliographic collections of the Biblioteca Biomédica (BB) SIIC.
Esta revista, clasificada por SIIC Data Bases,
integra el acervo bibliográfico de la Biblioteca Biomédica (BB) SIIC.
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Principal institution where the research took place
Institución principal de la investigación
University of Rome Tor Vergata, Rome, Rome, Italy


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Authors' Report

Crónica del Autor
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Bibliographic references
Referencias bibliográficas

Adler V, Yin Z, Tew KD, Ronai Z. Role of redox potential and reactive oxygen species in stress signaling. Oncogene 18:6104-6111, 1999.
Benezra R. An intermolecular disulfide bond stabilizes E2A homodimers and is required for DNA binding at physiological temperatures. Cell 79:1057-1067, 1994.
Bentires-Alj M, Paez JG, David FS, Keilhack H, Halmos B, Naoki K, et al. Activating mutations of the noonan syndrome-associated SHP2/PTPN11 gene in human solid tumors and adult acute myelogenous leukemia. Cancer Res 64:8816-8820, 2004.
Dance M, Montagner A, Salles JP, Yart A, Raynal P. The molecular functions of Shp2 in the Ras/Mitogen-activated protein kinase (ERK1/2) pathway. Cell Signal 20:453-459, 2008.
Finkel T. Oxygen radicals and signaling. Curr Opin Cell Biol 10:248-253, 1998.
Huang Q, Lerner-Marmarosh N, Che W, Ohta S, Osawa M, Yoshizumi M, et al. The novel role of the C-terminal region of SHP-2. Involvement of Gab1 and SHP-2 phosphatase activity in Elk-1 activation. J Biol Chem 277:29330-29341, 2002.
Legius E, Schrander-Stumpel C, Schollen E, Pulles-Heintzberger C, Gewillig M, Fryns JP. PTPN11 mutations in LEOPARD syndrome. J Med Genet 39:571-574, 2002.
Lesage F, Reyes R, Fink M, Duprat F, Guillemare E, Lazdunski M. Dimerization of TWIK-1 K+ channel subunits via a disulfide bridge. EMBO J 15:6400-6407, 1996.
Martinelli S, Nardozza AP, Delle Vigne S, Sabetta G, Torreri P, Bocchinfuso G, et al. Counteracting effects operating on Src-homology 2 domain-containing protein tyrosine phosphatase 2 (SHP2) function drive selection of the recurrent Y62D and Y63C substitutions in Noonan syndrome. J Biol Chem 287(32):27066-27077, 2012.
Martinelli S, Torreri P, Tinti M, Stella L, Bocchinfuso G, Flex E, et al. Diverse driving forces underlie the invariant occurrence of the T42A, E139D, I282V and T468M SHP2 amino acid substitutions causing Noonan and LEOPARD syndromes. Hum Mol Genet 17:2018-2029, 2008.
Meng TC, Fukada T, Tonks NK. Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo. Mol Cell 9:387-399, 2002.
Mesecke N, Terziyska N, Kozany C, Baumann F, Neupert W, Hell K, Herrmann JM. A disulfide relay system in the intermembrane space of mitochondria that mediates protein import. Cell 121:1059-1069, 2005.
Tartaglia M, Martinelli S, Stella L, Bocchinfuso G, Flex E, Cordeddu V, et al. Diversity and functional consequences of germline and somatic PTPN11 mutations in human disease. Am J Hum Genet 78:279-290, 2006.
Tartaglia M, Mehler EL, Goldberg R, Zampino G, Brunner HG, Kremer H, et al. Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome. Nat Genet 29:465-468, 2001.
Tartaglia M, Niemeyer CM, Fragale A, Song X, Buechner J, Jung A, et al. Somatic mutations in PTPN11 in juvenile myelomonocytic leukemia, myelodysplastic syndromes and acute myeloid leukemia. Nat Genet 34:148-150, 2003.

Other articles written by the author Aurelio Pio Nardozza
Otros artículos de Aurelio Pio Nardozza





SIIC System of Assisted Editing (SSEA)
/ Sistema SIIC de Edición Asistida (SSEA)

Aurelio Pio Nardozza was invited by SIIC on
Aurelio Pio Nardozza fue invitado por SIIC el
2012, august 23
  The authors' report was accepted on
La crónica del autor fue aprobada el
2013, april 27
The authors' report was accepted on
La crónica del autor fue aprobada el
2013, april 27
Published in siicsalud
Publicado en siicsalud
2013, july 26





The article is strictly related to the following sections of siicsalud
El artículo se relaciona estrictamente con las siguientes secciones de siicsalud

 
Biochemistry
/ Bioquímica
 
Genetics
/ Genética Humana
 

and secondarily related to the following sections

y secundariamente con las siguientes secciones

Molecular Biology
Biología Molecular

Genetic Biochemistry
Bioquímica Genética

Biological Chemistry
Química Biológica

Information about the full text
Acerca del trabajo completo


Reactive Oxygen Species and Epidermal Growth Factor Are Antagonistic Cues Controlling SHP-2 Dimerization


Author / Autor
Aurelio Pio Nardozza1, Melania D'orazio2, Riccardo Trapannone3, Salvatore Corallino4, Giuseppe Filomeni5, Marco Tartaglia6, Andrea Battistoni7, Gianni Cesareni8, Luisa Castagnoli9

9, University Of Rome Tor Vergata


Access to the original source
Molecular and Cellular Biology

Article URL:
/ URL del artículo:
http://mcb.asm.org/

URL of Abstract:
/ URL del abstract:
http://mcb.asm.org/search?fulltext=nardozza&submit=yes&x=0&y=0

URL of Abstract page in Medline:
/ URL del abstract en Medline:
http://www.ncbi.nlm.nih.gov/pubmed/22411627

URL of Abstract page in Scielo:
/ URL del abstract en Scielo:

URL of Abstract page in Scopus:
/ URL del abstract en Scopus:

URL of Abstract page in Embase:
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Other data bases:
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siic DB:
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http://www.siicsalud.com/main/distriprinrel.php
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