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J Biol Chem, Vol. 273, Issue 38, 24301-24304, September 18, 1998

COMMUNICATION
Grb2 Interaction with MEK-Kinase 1 Is Involved in Regulation of Jun-Kinase Activities in Response to Epidermal Growth Factor

Martine Pomérance, Marie-Christine Multon^¶, Fabienne Parker^¶, Corinne Venot^¶, Jean-Paul Blondeau, Bruno Tocqué, and Fabien Schweighoffer

From the  Unité 486 INSERM, Transduction Hormonale et Régulation Cellulaire, Faculté de Pharmacie, 92296 Châtenay-Malabry, France, the ^¶ Rhône-Poulenc Rorer, Centre de Recherche de Vitry-Alfortville, 13 quai Jules Guesde, BP14, 94403 Vitry sur Seine, France, and  Exonhit Therapeutics, 65 Bd Masséna, 75013 Paris, France

Epidermal growth factor (EGF) receptor was shown to be involved in the activation pathway of the stress-activated protein kinase/c-Jun NH₂-terminal kinase (SAPK/JNK) cascade not only by EGF, but also by UV radiation or osmotic stress. This paper describes a specific interaction between the COOH-terminal SH3 domain of Grb2 and the NH₂-terminal regulatory domain of MEKK1 in ER22 cells overexpressing the EGF receptor. This interaction results in the formation of a constitutive complex between Grb2 and MEKK1 in both proliferating and resting cells. EGF stimulation causes this complex to be rapidly and transiently recruited by Shc proteins. The subsequent release of the Grb2-MEKK1 complex from Shc proteins correlates with JNK activation. Transfection of the NH₂-terminal regulatory domain of MEKK1 specifically inhibits EGF-dependent JNK activation indicating that Grb2 is involved in MEKK1 activation. Thus, adaptor proteins have a new role in the regulation of the SAPK/JNK cascade after EGF stimulation.

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