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Withdrawal: hSos1 contains a new amino-terminal regulatory motif with specific binding affinity for its pleckstrin homology domain.

Open AccessPublished:July 20, 2018DOI:https://doi.org/10.1074/jbc.W118.004643
      VOLUME 277 (2002) PAGES 44171–44179
      This article has been withdrawn by the authors (although Rocío Jorge could not be reached and Natalia Martínez passed away). The authors have become aware of errors in the preparation of Figs. 2A, 3A, 4A, and 5A, where some lanes appear to be duplicated. The authors state that although replicated experiments performed at the time of the article as well as subsequent data published by other groups (Sondermann, H., Nagar, B., Bar-Sagi, D., and Kuriyan, J. (2005) Computational docking and solution x-ray scattering predict a membrane-interacting role for the histone domain of the Ras activator son of sevenless. Proc. Natl. Acad. Sci. U.S.A. 102, 16632–16637; Yadav, K. K., and Bar-Sagi, D. (2010) Allosteric gating of Son of sevenless activity by the histone domain. Proc. Natl. Acad. Sci. U.S.A. 107, 3436–3440; and Tartaglia, M., Pennacchio, L. A., Zhao, C., Yadav, K. K., Fodale, V., Sarkozy, A., Pandit, B., Oishi, K., Martinelli, S., Schackwitz, W., Ustaszewska, A., Martin, J., Bristow, J., Carta, C., Lepri, F., Neri, C., Vasta, I., Gibson, K., Curry, C. J., Siguero, J. P., Digilio, M. C., Zampino, G., Dallapiccola, B., Bar-Sagi, D., and Gelb, B. D. (2007) Nat. Genet. 39, 75–79) support the results and conclusions presented in this published paper, they consider that the responsible course of action is to withdraw the article in the interests of maintaining the publication standards of the journal. The authors apologize for any inconvenience they may have caused. The paper with the corrected figures can be obtained by contacting the authors.

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      • hSos1 Contains a New Amino-terminal Regulatory Motif with Specific Binding Affinity for Its Pleckstrin Homology Domain
        Journal of Biological ChemistryVol. 277Issue 46
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          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.
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