Cited by 468Protein Kinase Regulation and GTPase SignalingDevelopmental Biology and Gene RegulationAxon Guidance and Neuronal Signaling

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Sprouty, an Intracellular Inhibitor of Ras Signaling

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Casci, Tanita, Vinós, Javier, Freeman, Matthew·1999·Cell

DOI 10.1016/s0092-8674(00)80576-0

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Abstract

Sprouty was identified in a genetic screen as an inhibitor of Drosophila EGF receptor signaling. The Egfr triggers cell recruitment in the eye, and sprouty- eyes have excess photoreceptors, cone cells, and pigment cells. Sprouty's function is, however, more widespread. We show that it also interacts genetically with the receptor tyrosine kinases Torso and Sevenless, and it was first discovered through its effect on FGF receptor signaling. In contrast to an earlier proposal that Sprouty is extracellular, we show by biochemical analysis that Sprouty is an intracellular protein, associated with the inner surface of the plasma membrane. Sprouty binds to two intracellular components of the Ras pathway, Drk and Gap1. Our results indicate that Sprouty is a widespread inhibitor of Ras pathway signal transduction.

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Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
Nielsen, H., Engelbrecht, J., Brunak, S., & von HEIJNE, G. (1997) · Protein Engineering Design and Selection · doi:10.1093/protein/10.1.1 · Cited by 5,343
Analysis of genetic mosaics in developing and adult Drosophila tissues
Xu, T., & Rubin, G. M. (1993) · Development · doi:10.1242/dev.117.4.1223 · Cited by 2,066
The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling
Lowenstein, E. J., Daly, R. J., Batzer, A., Li, W., Margolis, B. L., Lammers, R., Ullrich, A., Skolnik, E. Y., Bar‐Sagi, D., & Schlessinger, J. (1992) · Cell · doi:10.1016/0092-8674(92)90167-b · Cited by 1,632
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Bhanot, P., van den Brink, M. R. M., Samos, C. H., Hsieh, J.-C., Wang, Y., Macke, J. P., Andrew, D. J., Nathans, J., & Nusse, R. (1996) · Nature · doi:10.1038/382225a0 · Cited by 1,504
Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos nucleotide exchange factor
Buday, L., & Downward, J. (1993) · Cell · doi:10.1016/0092-8674(93)90146-h · Cited by 1,064
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Leevers, S. J., Paterson, H. F., & Marshall, C. J. (1994) · Nature · doi:10.1038/369411a0 · Cited by 1,011
Activation of Raf as a Result of Recruitment to the Plasma Membrane
Stokoe, D., Macdonald, S. G., Cadwallader, K. A., Symons, M. H., & Hancock, J. F. (1994) · Science · doi:10.1126/science.7811320 · Cited by 976
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Authors: Casci, T., Vinós, J., & Freeman, M.
Affiliations: MRC Laboratory of Molecular Biology (GB)
Corresponding author: Freeman, Matthew
ORCID: Casci, Tanita
Freeman, Matthew
Venue: Cell
Publisher: Elsevier BV
Published: 1999-03
Volume: 96
Issue: 5
Pages: 655-665
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/s0092-8674(00)80576-0
OpenAlex: W2082773871
Cited by: 467
References: 62
Citations by year: 2026: 2 · 2025: 2 · 2024: 5 · 2023: 8 · 2022: 8 · 2021: 13 · 2020: 13 · 2019: 4 · 2018: 10 · 2017: 11 · 2016: 19 · 2015: 16 · 2014: 12 · 2013: 15 · 2012: 17
FWCI: 10.93
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 5252 d)
Locations: Cell (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Axon Guidance and Neuronal Signaling
Keywords: Sprouty, Ras signaling, EGF receptor signaling, Drosophila, Torso receptor, FGF receptor signaling, DRK, GAP1, receptor tyrosine kinase, pigment cells, plasma membrane
MeSH terms: Animals, Cells, Cultured, Cysteine, Depression, Chemical, Drosophila melanogaster, Eye, Eye Abnormalities, Eye Proteins, Membrane Glycoproteins, Membrane Proteins, Morphogenesis, Proteins, Signal Transduction, ras Proteins, Insect Proteins, ras GTPase-Activating Proteins, Receptor Protein-Tyrosine Kinases, Drosophila Proteins, Macromolecular Substances, ErbB Receptors

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Sprouty, an Intracellular Inhibitor of Ras Signaling

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