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Grb2 and its apoptotic isoform Grb3-3 associate with heterogeneous nuclear ribonucleoprotein C, and these interactions are modulated by Poly(U) RNA

AuthorsRomero, Francisco; Ramos-Morales, Francisco; Domínguez, África; Ríos, Rosa M. ; Schweighoffer, F.; Tocqué, B.; Pintor-Toro, José Antonio ; Tortolero, María
Issue Date1998
PublisherAmerican Society for Biochemistry and Molecular Biology
CitationJournal of Biological Chemistry 273: 7776-7781 (1998)
AbstractGrb2 is an adaptor molecule comprising one Src homology (SH) 2 and two SH3 domains. This protein has a natural isoform named Grb3-3 with a deletion within the Sh2 domain. Numerous evidence points to a functional connection between SH2- and SH3-containing proteins and molecules implicated in RNA biogenesis. In this context, we have examined the binding of Grb2 and Grb3-3 to heterogeneous nuclear ribonucleoprotein (hnRNP) C. By the use of an in vivo genetic approach the through in vitro experiments, we furnish evidence that both Grb2 and Grb3-3 interact with hnRNP C proteins. Subcellular fractionation studies clearly show that Grb2 is partially localized in the nucleus. In addition, coimmunoprecipitation experiments demonstrate that Grb2·hnRNP C complexes exist in intact hematopoietic cells. The carboxyl- terminal SH3 domain of Grb2 and Grb3-3 are primarily responsible for the association with hnRNP C. However, although the proline-rich motif of hnRNP C is involved in the interaction with Grb2, it is not in the binding to Grb3- 3. Furthermore, poly(U) NRA inhibits the association of Grb2 with hnRNP C, whereas it enhances the interaction between Grb3-3 and hnRNP C. These findings suggest that the Grb2/Grb3-3-hnRNP C interactions might fulfill different biological functions.
Identifiersdoi: 10.1074/jbc.273.13.7776
issn: 0021-9258
e-issn: 1083-351X
Appears in Collections:(IRNAS) Artículos
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