Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 28 April 1995:
Vol. 268. no. 5210, pp. 576 - 579
DOI: 10.1126/science.7725106
Prev | Table of Contents | Next

Articles

Science, Vol 268, Issue 5210, 576-579
Copyright © 1995 by American Association for the Advancement of Science

articles

In vivo functional analysis of the Ras exchange factor son of sevenless

CA Karlovich, L Bonfini, L McCollam, RD Rogge, A Daga, MP Czech, and U Banerjee

Department of Biology and Molecular Biology Institute, University of California, Los Angeles 90024, USA.

The Son of sevenless (Sos) protein functions as a guanine nucleotide transfer factor for Ras and interacts with the receptor tyrosine kinase Sevenless through the protein Drk, a homolog of mammalian Grb2. In vivo structure-function analysis revealed that the amino terminus of Sos was essential for its function in flies. A molecule lacking the amino terminus was a potent dominant negative. In contrast, a Sos fragment lacking the Drk binding sites was functional and its activity was dependent on the presence of the Sevenless receptor. Furthermore, membrane localization of Sos was independent of Drk. A possible role for Drk as an activator of Sos is discussed and a Drk-independent interaction between Sos and Sevenless is proposed that is likely mediated by the pleckstrin homology domain within the amino terminus.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Germ Line Gain of Function with SOS1 Mutation in Hereditary Gingival Fibromatosis.
S.-I. Jang, E.-J. Lee, P. S. Hart, M. Ramaswami, D. Pallos, and T. C. Hart (2007)
J. Biol. Chem. 282, 20245-20255
   Abstract »    Full Text »    PDF »
An Activating Mutation in sos-1 Identifies Its Dbl Domain as a Critical Inhibitor of the Epidermal Growth Factor Receptor Pathway during Caenorhabditis elegans Vulval Development.
K. Modzelewska, M. G. Elgort, J. Huang, G. Jongeward, A. Lauritzen, C. H. Yoon, P. W. Sternberg, and N. Moghal (2007)
Mol. Cell. Biol. 27, 3695-3707
   Abstract »    Full Text »    PDF »
Signaling Mechanisms Regulating Endothelial Permeability.
D. Mehta and A. B. Malik (2006)
Physiol Rev 86, 279-367
   Abstract »    Full Text »    PDF »
hSos1 Contains a New Amino-terminal Regulatory Motif with Specific Binding Affinity for Its Pleckstrin Homology Domain.
R. Jorge, N. Zarich, J. L. Oliva, M. Azanedo, N. Martinez, X. de la Cruz, and J. M. Rojas (2002)
J. Biol. Chem. 277, 44171-44179
   Abstract »    Full Text »    PDF »
The Multisubstrate Adapter Gab1 Regulates Hepatocyte Growth Factor (Scatter Factor)-c-Met Signaling for Cell Survival and DNA Repair.
S. Fan, Y. X. Ma, M. Gao, R.-Q. Yuan, Q. Meng, I. D. Goldberg, and E. M. Rosen (2001)
Mol. Cell. Biol. 21, 4968-4984
   Abstract »    Full Text »    PDF »
Calmodulin and son of sevenless dependent signaling pathways regulate midline crossing of axons in the Drosophila CNS.
J. Fritz and M. VanBerkum (2000)
Development 127, 1991-2000
   Abstract »    PDF »
Rasputin, the Drosophila homologue of the RasGAP SH3 binding protein, functions in ras- and Rho-mediated signaling.
C Pazman, C. Mayes, M Fanto, S. Haynes, and M Mlodzik (2000)
Development 127, 1715-1725
   Abstract »    PDF »
Insulin-induced Desensitization of Extracellular Signal-regulated Kinase Activation Results from an Inhibition of Raf Activity Independent of Ras Activation and Dissociation of the Grb2-SOS Complex.
R. V. Fucini, S. Okada, and J. E. Pessin (1999)
J. Biol. Chem. 274, 18651-18658
   Abstract »    Full Text »    PDF »
Disabled Is a Putative Adaptor Protein That Functions during Signaling by the Sevenless Receptor Tyrosine Kinase.
N. Le and M. A. Simon (1998)
Mol. Cell. Biol. 18, 4844-4854
   Abstract »    Full Text »
N Terminus of Sos1 Ras Exchange Factor: Critical Roles for the Dbl and Pleckstrin Homology Domains.
X. Qian, W. C. Vass, A. G. Papageorge, P. H. Anborgh, and D. R. Lowy (1998)
Mol. Cell. Biol. 18, 771-778
   Abstract »    Full Text »
Regulation of Sos Activity by Intramolecular Interactions.
S. Corbalan-Garcia, S. M. Margarit, D. Galron, S.-s. Yang, and D. Bar-Sagi (1998)
Mol. Cell. Biol. 18, 880-886
   Abstract »    Full Text »
Protein Kinase D Activation by Mutations within Its Pleckstrin Homology Domain.
T. Iglesias and E. Rozengurt (1998)
J. Biol. Chem. 273, 410-416
   Abstract »    Full Text »    PDF »
The Solution Structure of the Pleckstrin Homology Domain of Human SOS1. A POSSIBLE STRUCTURAL ROLE FOR THE SEQUENTIAL ASSOCIATION OF DIFFUSE B CELL LYMPHOMA AND PLECKSTRIN HOMOLOGY DOMAINS.
J. Zheng, R.-H. Chen, S. Corblan-Garcia, S. M. Cahill, D. Bar-Sagi, and D. Cowburn (1997)
J. Biol. Chem. 272, 30340-30344
   Abstract »    Full Text »    PDF »
Requirement for Drosophila 14-3-3 zeta in Raf-dependent photoreceptor development..
L Kockel, G Vorbruggen, H Jackle, M Mlodzik, and D Bohmann (1997)
Genes & Dev. 11, 1140-1147
   Abstract »    PDF »
Mutation in Sos1 dominantly enhances a weak allele of the EGFR, demonstrating a requirement for Sos1 in EGFR signaling and development..
D Z Wang, V E Hammond, H E Abud, I Bertoncello, J W McAvoy, and D D Bowtell (1997)
Genes & Dev. 11, 309-320
   Abstract »    PDF »
High Affinity Binding of the Pleckstrin Homology Domain of mSos1 to Phosphatidylinositol (4,5)-Bisphosphate.
T. J. Kubiseski, Y. M. Chook, W. E. Parris, M. Rozakis-Adcock, and T. Pawson (1997)
J. Biol. Chem. 272, 1799-1804
   Abstract »    Full Text »    PDF »
klingon, a novel member of the Drosophila immunoglobulin superfamily, is required for the development of the R7 photoreceptor neuron.
S. Butler, S Ray, and Y Hiromi (1997)
Development 124, 781-792
   Abstract »    PDF »
The Grb2-mSos1 Complex Binds Phosphopeptides with Higher Affinity than Grb2.
Y. M. Chook, G. D. Gish, C. M. Kay, E. F. Pai, and T. Pawson (1996)
J. Biol. Chem. 271, 30472-30478
   Abstract »    Full Text »    PDF »
Interactions between Src Homology (SH) 2/SH3 Adapter Proteins and the Guanylnucleotide Exchange Factor SOS Are Differentially Regulated by Insulin and Epidermal Growth Factor.
S. Okada and J. E. Pessin (1996)
J. Biol. Chem. 271, 25533-25538
   Abstract »    Full Text »    PDF »
Insulin and Epidermal Growth Factor Receptors Regulate Distinct Pools of Grb2-SOS in the Control of Ras Activation.
S. B. Waters, D. Chen, A. W. Kao, S. Okada, K. H. Holt, and J. E. Pessin (1996)
J. Biol. Chem. 271, 18224-18230
   Abstract »    Full Text »    PDF »
Isolated Sos1 PH Domain Exhibits Germinal Vesicle Breakdown-inducing Activity in Xenopus Oocytes.
J. F. d. Mora, C. Guerrero, D. Mahadevan, J. J.R. Coque, J. M. Rojas, L. M. Esteban, M. Rebecchi, and E. Santos (1996)
J. Biol. Chem. 271, 18272-18276
   Abstract »    Full Text »    PDF »
Epidermal Growth Factor Receptor Targeting Prevents Uncoupling of the Grb2-SOS Complex.
K. H. Holt, S. B. Waters, S. Okada, K. Yamauchi, S. J. Decker, A. R. Saltiel, D. G. Motto, G. A. Koretzky, and J. E. Pessin (1996)
J. Biol. Chem. 271, 8300-8306
   Abstract »    Full Text »    PDF »
Functional Roles for the Pleckstrin and Dbl Homology Regions in the Ras Exchange Factor Son-of-sevenless.
L. McCollam, L. Bonfini, C. A. Karlovich, B. R. Conway, L. M. Kozma, U. Banerjee, and M. P. Czech (1995)
J. Biol. Chem. 270, 15954-15957
   Abstract »    Full Text »    PDF »
Tyrosine-phosphorylated Low Density Lipoprotein Receptor-related Protein 1 (LRP1) Associates with the Adaptor Protein SHC in SRC-transformed Cells.
H. Barnes, B. Larsen, M. Tyers, and P. van der Geer (2001)
J. Biol. Chem. 276, 19119-19125
   Abstract »    Full Text »    PDF »
Structure-based Mutagenesis Reveals Distinct Functions for Ras Switch 1 and Switch 2 in Sos-catalyzed Guanine Nucleotide Exchange.
B. E. Hall, S. S. Yang, P. A. Boriack-Sjodin, J. Kuriyan, and D. Bar-Sagi (2001)
J. Biol. Chem. 276, 27629-27637
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)