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J Biol Chem, Vol. 273, Issue 13, 7776-7781, March 27, 1998

Grb2 and Its Apoptotic Isoform Grb3-3 Associate with Heterogeneous Nuclear Ribonucleoprotein C, and These Interactions Are Modulated by Poly(U) RNA

Francisco Romero, Francisco Ramos-Morales^¶, Africa Domínguez^¶, Rosa María Rios^¶, Fabien Schweighoffer, Bruno Tocqué, José Antonio Pintor-Toro^**, Siegmund Fischer, and María Tortolero^¶

From the  Institut Cochin de Génétique Moléculaire, U363 INSERM, Hôpital Cochin, 27 rue du faubourg Saint Jacques, 75014 Paris, France, ^¶ Departamento de Microbiología, Facultad de Biología, Universidad de Sevilla, Apdo. 1095, 41080 Sevilla, Spain,  Rhône-Poulenc-Rorer, Centre de Recherche de Vitry-Alfortville, 13 quai Jules Guesde-BP14, 94403 Vitry sur Seine Cedex, France, and ^** Instituto de Recursos Naturales y Agrobiología, Consejo Superior de Investigaciones Científicas, Apdo. 1052, 41080 Sevilla, Spain

Grb2 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 and 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 domains 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) RNA 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.

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