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Originally published In Press as doi:10.1074/jbc.M204423200 on September 9, 2002

J. Biol. Chem., Vol. 277, Issue 46, 44171-44179, November 15, 2002
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hSos1 Contains a New Amino-terminal Regulatory Motif with Specific Binding Affinity for Its Pleckstrin Homology Domain*

Rocío JorgeDagger §, Natasha ZarichDagger §, José Luis Oliva, Marta Azañedo, Natalia Martínez§, Xavier de la Cruz||**, and José M. RojasDagger Dagger

From the Unidad de Biología Celular, Centro Nacional de Microbiología, Instituto de Salud Carlos III, 28220 Majadahonda, Madrid, Spain, the || Departamento de Bioquímica y Biología Molecular, Facultad de Químicas, Universidad de Barcelona, 08028 Spain, and the ** Institut Catala de Recerca i Estudis Avançats (ICREA), 08028 Barcelona, Spain

The protein hSos1 is a Ras guanine nucleotide exchange factor. In the present study, we investigated the function of the amino-terminal region of the hSos1 protein, corresponding to the first 600 residues, which includes the Dbl and pleckstrin homology (DH and PH) domains. We demonstrated, using a series of truncated mutants, that this region is absolutely necessary for hSos1 activity. Our results suggest that the first 200 residues (upstream of DH domain), which we called the HF motif on the basis of their homology with histone H2A, may exert negative control over the functional activity of the whole hSos1 protein. In vitro binding analysis showed that the HF motif is able to interact specifically with the PH domain of hSos1. The amino-terminal region of hSos1 may be associated in vivo with an expressed HF motif. These findings document the existence of the HF motif located upstream of the DH domain in the hSos1 protein. This motif may be responsible for the negative control of hSos1, probably by intramolecular binding with the PH domain.

* This research was supported by grants from CAM (08.1/0003.1/99), PGC (PM99-0015), and Ratiopharm and by Intramural Grant ISCIII 01/16 (all to J. M. R.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Recipients of fellowships from AECC.

§ Recipients of fellowships from ISCIII.

Recipient of a fellowship from FIS-BEFI.

Dagger Dagger To whom correspondence should be addressed: Unidad de Biología Celular, Centro Nacional de Microbiología, Instituto de Salud Carlos III, carretera Majadahonda-Pozuelo, Km. 2, Majadahonda 28220, Madrid, Spain. Tel.: 34-91-509-7010; Fax: 34-91-509-7919; E-mail: jmrojas@isciii.es.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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