English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/64162
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:

Title

Adenosine deaminase is a specific partner for the Grb2 isoform Grb3-3

AuthorsRamos-Morales, Francisco; Domínguez, África; Ríos, Rosa M. ; Barroso, Sonia ; Infante, Carlos; Schweighoffer, F.; Tocqué, B.; Pintor-Toro, José Antonio ; Tortolero, María
Issue Date1997
PublisherAcademic Press
CitationBiochemical and Biophysical Research Communications 237(3): 735-740 (1997)
AbstractGrb3-3 is an isoform of Grb2, thought to arise by alternative splicing, that lacks a functional SH2 domain but retains functional SH3 domains, which allow interaction with other proteins through binding to prolinerich sequences. Several evidences suggest that besides common partners for Grb2 and Grb3-3, specific targets could exist. In order to find specific partners for Grb3-3, we have screened a human cDNA library by the yeast two-hybrid system with Grb3-3 as a bait. We have identified adenosine deaminase, an enzyme involved in purine metabolism whose deficiency is associated with severe combined immunodeficiency, as a Grb3-3 binding protein that is not able to bind to Grb2. This interaction has been confirmed in vitro with GST fusion proteins and in vivo by coimmunoprecipitation experiments in NIH3T3 cells stably transfected with Grb3-3. The functional significance of this finding is discussed.
URIhttp://hdl.handle.net/10261/64162
DOI10.1006/bbrc.1997.7221
Identifiersdoi: 10.1006/bbrc.1997.7221
issn: 0006-291X
Appears in Collections:(IRNAS) Artículos
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdf15,38 kBAdobe PDFThumbnail
View/Open
Show full item record
Review this work
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.