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Sprouty, an Intracellular Inhibitor of Ras Signaling
Open accessAbstract
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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“Four of the validated miR-21 target genes are known negative regulators of the Ras/MEK/ERK pathway: sprouty 1 (Spry1), sprouty 2 (Spry2), B-cell translocation gene 2 (Btg2), and programmed cell death 4 (Pdcd4).”
From Modulation of K-Ras-Dependent Lung Tumorigenesis by MicroRNA-21 (2010) · cites this paper as Casci et al., 1999
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Cites
Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
Brand, A. H., & Perrimon, N. (1993) · Development · doi:10.1242/dev.118.2.401 · Cited by 9,510
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
A new member of the frizzled family from Drosophila functions as a Wingless receptor
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
Buday, L., & Downward, J. (1993) · Cell · doi:10.1016/0092-8674(93)90146-h · Cited by 1,064
Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane
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
Reiterative Use of the EGF Receptor Triggers Differentiation of All Cell Types in the Drosophila Eye
Freeman, M. (1996) · Cell · doi:10.1016/s0092-8674(00)81385-9 · Cited by 877
Self-citationSimon, M. A., Bowtell, D. D. L., Dodson, G. S., Laverty, T., & Rubin, G. M. (1991) · Cell · doi:10.1016/0092-8674(91)90065-7 · Cited by 860
Cited by
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Olson, M. F., & Marais, R. (2000) · Seminars in Immunology · doi:10.1006/smim.2000.0208 · Cited by 124
Mason, J. M., Morrison, D. J., Bassit, B., Dimri, M., Band, H., Licht, J. D., & Groß, I. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-07-0503 · Cited by 125
RetractedLee, C.-C., Putnam, A. J., Miranti, C. K., Gustafson, M. F., Wang, L.-M., Woude, G. F. V., & Gao, C.-F. (2004) · Oncogene · doi:10.1038/sj.onc.1207646 · Cited by 124
Molecular and Cellular Basis of Regeneration and Tissue Repair
Slack, J. M. W., Lin, G., & Chen, Y. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7431-1 · Cited by 122
Pai, L., Barcelo, G., & Schüpbach, T. (2000) · Cell · doi:10.1016/s0092-8674(00)00104-5 · Cited by 122
Tran, H., Hamada, F., Schwarz, T., & Bienz, M. (2008) · Genes & Development · doi:10.1101/gad.463208 · Cited by 122
Kwabi‐Addo, B., Wang, J., Erdem, H., Vaid, A., Castro, P. D., Ayala, G., & Ittmann, M. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-3759 · Cited by 119
Molecular cloning of mammalian Spred-3 which suppresses tyrosine kinase-mediated Erk activation
Kato, R., Nonami, A., Taketomi, T., Wakioka, T., Kuroiwa, A., Matsuda, Y., & Yoshimura, A. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00259-6 · Cited by 118
mSprouty2 inhibits FGF10-activated MAP kinase by differentially binding to upstream target proteins
Tefft, D., Lee, M., Smith, S. M., Crowe, D. L., Bellusci, S., & Warburton, D. (2002) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00372.2001 · Cited by 118
Fibroblast growth factors as tissue repair and regeneration therapeutics
Nunes, Q. M., Li, Y., Sun, C., Kinnunen, T. K., & Fernig, D. G. (2016) · PeerJ · doi:10.7717/peerj.1535 · Cited by 120
Sutterlüty, H., Mayer, C., Setinek, U., Attems, J., Ovtcharov, S., Mikula, M., Mikulits, W., Micksche, M., & Berger, W. (2007) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-06-0273 · Cited by 115
Chi, L., Zhang, S., Lin, Y., Prunskaite‐Hyyryläinen, R., Vuolteenaho, R., Itäranta, P., & Vainio, S. J. (2004) · Development · doi:10.1242/dev.01200 · Cited by 115
Epigenetic inactivation of the human sprouty2 (hSPRY2) homologue in prostate cancer
McKie, A. B., Douglas, D. A., Olijslagers, S., Graham, J. B., Omar, M. M., Heer, R., Gnanapragasam, V. J., Robson, C. N., & Leung, H. Y. (2005) · Oncogene · doi:10.1038/sj.onc.1208371 · Cited by 114
ERK Pathway Positively Regulates the Expression of Sprouty Genes
Ozaki, K., Kadomoto, R., Asato, K., Tanimura, S., Itoh, N., & Kohno, M. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5295 · Cited by 113
Intermolecular Interactions of Sprouty Proteins and Their Implications in Development and Disease
Edwin, F., Anderson, K. M., Ying, C., & Patel, T. B. (2009) · Molecular Pharmacology · doi:10.1124/mol.109.055848 · Cited by 116
Fibrosis in the lens. Sprouty regulation of TGFβ-signaling prevents lens EMT leading to cataract
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Halfar, K., Rommel, C., Stocker, H., & Hafen, E. (2001) · Development · doi:10.1242/dev.128.9.1687 · Cited by 109
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Differentially regulated and evolved genes in the fully sequenced Xq/Yq pseudoautosomal region
Ciccodicola, A. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.3.395 · Cited by 101
Lim, J., Wong, E. S. M., Ong, S. H., Yusoff, P., Low, B. C., & Guy, G. R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002156200 · Cited by 101
Targeting Fibroblast Growth Factor Pathways in Prostate Cancer
Corn, P. G., Wang, F., McKeehan, W. L., & Navone, N. M. (2013) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-1550 · Cited by 99
Human sprouty 4, a new ras antagonist on 5q31, interacts with the dual specificity kinase TESK1
Leeksma, O., van Achterberg, T. A. E., Tsumura, Y., Toshima, J., Eldering, E., Kroes, W. G. M., Mellink, C. H. M., Spaargaren, M., Mizuno, K., Pannekoek, H., et al. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.02921.x · Cited by 99
Genetic and Teratogenic Approaches To Craniofacial Development
Young, D., Schneider, R. A., Hu, D. P., & Helms, J. A. (2000) · Critical Reviews in Oral Biology & Medicine · doi:10.1177/10454411000110030201 · Cited by 98
Nonami, A., Kato, R., Taniguchi, K., Yoshiga, D., Taketomi, T., Fukuyama, S., Harada, M., Sasaki, A. T., & Yoshimura, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405189200 · Cited by 97
Regulation of EphB2 activation and cell repulsion by feedback control of the MAPK pathway
Poliakov, A. A., Cotrina, M. L., Pasini, A., & Wilkinson, D. G. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200807151 · Cited by 97
Tennis, M. A., Scoyk, M. M. V., Freeman, S. V., Vandervest, K. M., Nemenoff, R. A., & Winn, R. A. (2010) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-09-0400 · Cited by 97
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Denayer, E., Ahmed, T., Brems, H., van Woerden, G. M., Borgesius, N. Z., Callaerts‐Vegh, Z., Yoshimura, A., Hartmann, D., Elgersma, Y., D’Hooge, R., et al. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.4698-08.2008 · Cited by 97
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Lotsberg, M. L., Wnuk-Lipińska, K., Terry, S., Tan, T. Z., Lü, N., Trachsel-Moncho, L., Røsland, G. V., Siraji, M. I., Hellesøy, M., Rayford, A. J., et al. (2020) · Journal of Thoracic Oncology · doi:10.1016/j.jtho.2020.01.015 · Cited by 95
Miyoshi, K., Wakioka, T., Nishinakamura, H., Kamio, M., Yang, L., Inoue, M., Hasegawa, M., Yonemitsu, Y., Komiya, S., & Yoshimura, A. (2004) · Oncogene · doi:10.1038/sj.onc.1207759 · Cited by 93
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Rubin, C., Gur, G., & Yarden, Y. (2005) · Cell Research · doi:10.1038/sj.cr.7290268 · Cited by 91
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Guy, G. R., Wong, E. S. M., Yusoff, P., Chandramouli, S., Lo, T. L., Lim, J., & Fong, C. W. (2003) · Journal of Cell Science · doi:10.1242/jcs.00652 · Cited by 90
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Lo, T. L., Fong, C. W., Yusoff, P., McKie, A. B., Chua, M., Leung, H. Y., & Guy, G. R. (2006) · Cancer Letters · doi:10.1016/j.canlet.2005.12.032 · Cited by 89
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Kim, S. ‐., Hu, Y., Cadman, S., & Bouloux, P. (2008) · Journal of Neuroendocrinology · doi:10.1111/j.1365-2826.2007.01627.x · Cited by 87
Giacomini, A., Chiodelli, P., Matarazzo, S., Rusnati, M., Presta, M., & Ronca, R. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.03.024 · Cited by 89
Feedback regulation of RTK signaling in development
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Depew, M. J., & Simpson, C. A. (2006) · Developmental Dynamics · doi:10.1002/dvdy.20796 · Cited by 82
Kumar, J. P., & Moses, K. (2001) · Development · doi:10.1242/dev.128.14.2689 · Cited by 82
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DaSilva, J. O., Xu, L., Kim, H. J., Miller, W. T., & Bar‐Sagi, D. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.5.1898-1907.2006 · Cited by 83
Xiong, S., Zhao, Q., Rong, Z., Huang, G., Huang, Y., Chen, P., Zhang, S., Liu, L., & Chang, Z. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306936200 · Cited by 85
Groß, I., Morrison, D. J., Hyink, D. P., Georgas, K. M., English, M. A., Mericskay, M., Hosono, S., Sassoon, D. A., Wilson, P. D., Little, M. H., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306425200 · Cited by 82
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Giacomini, A., Grillo, E., Rezzola, S., Ribatti, D., Rusnati, M., Ronca, R., & Presta, M. (2020) · Physiological Reviews · doi:10.1152/physrev.00005.2020 · Cited by 81
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RetractedZhang, C., Wang, H., Liu, X., Hu, Y., Lei, D., Zhang, X., Sun, Q., & Li, Y. (2018) · Oncogene · doi:10.1038/s41388-018-0534-3 · Cited by 79
Comparative Mechanisms of Branching Morphogenesis in Diverse Systems
Lu, P., Sternlicht, M. D., & Werb, Z. (2006) · Journal of Mammary Gland Biology and Neoplasia · doi:10.1007/s10911-006-9027-z · Cited by 79
Wang, J., Thompson, B., Ren, C., Ittmann, M., & Kwabi‐Addo, B. (2005) · The Prostate · doi:10.1002/pros.20353 · Cited by 77
Role of fibroblast growth factor 8 in growth and progression of hormonal cancer
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Aranda, S., Álvarez, M., Turró, S., Laguna, A., & de la Luna, S. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00394-08 · Cited by 76
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Bertrand, N., Médevielle, F., & Pituello, F. (2000) · Development · doi:10.1242/dev.127.22.4837 · Cited by 75
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Shilo, B. (2014) · Methods · doi:10.1016/j.ymeth.2014.01.020 · Cited by 72
Regulation of Sprouty2 stability by mammalian Seven‐in‐Absentia homolog 2
Nadeau, R. J., Toher, J. L., Yang, X., Kovalenko, D., & Friesel, R. E. (2006) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21040 · Cited by 74
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Nobuhisa, I., Kato, R., Inoue, H., Takizawa, M., Okita, K., Yoshimura, A., & Taga, T. (2004) · The Journal of Experimental Medicine · doi:10.1084/jem.20030830 · Cited by 71
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Xian, W., Schwertfeger, K. L., & Rosen, J. M. (2007) · Molecular Endocrinology · doi:10.1210/me.2006-0518 · Cited by 70
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Sprouty proteins are in vivo targets of Corkscrew/SHP-2 tyrosine phosphatases
Jarvis, L. A., Peters, S. T., Simon, M. A., Krasnow, M. A., & Smith-Bolton, R. K. (2006) · Development · doi:10.1242/dev.02255 · Cited by 69
Johnston, I., Spence, H. J., Winnie, J. N., McGarry, L., Vass, J. K., Meagher, L., Stapleton, G., & Ozanne, B. W. (2000) · Oncogene · doi:10.1038/sj.onc.1203927 · Cited by 69
Lao, D.-H., Chandramouli, S., Yusoff, P., Fong, C. W., Saw, T. Y., Tai, L. P., Yu, C. Y., Leong, H. F., & Guy, G. R. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604044200 · Cited by 68
Lin, W., Fürthauer, M., Thisse, B., Thisse, C., Jing, N., & Ang, S. (2002) · Mechanisms of Development · doi:10.1016/s0925-4773(02)00018-7 · Cited by 68
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Ohshiro, T., Emori, Y., & Saigo, K. (2002) · Mechanisms of Development · doi:10.1016/s0925-4773(02)00042-4 · Cited by 67
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Lei, Z., van Mil, A., Brandt, M. M., Grundmann, S., Hoefer, I., Smits, M., el Azzouzi, H., Fukao, T., Cheng, C., Doevendans, P. A., et al. (2015) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12586 · Cited by 58
Ghiglione, C., Amundadottir, L. T., Andrésdóttir, M. B., Bilder, D. H., Diamonti, J. A., Noselli, S., Perrimon, N., & Carraway, K. L. (2003) · Development · doi:10.1242/dev.00617 · Cited by 65
Bai, J.-M., Chiu, W.-H., Wang, J.-C., Tzeng, T.-H., Perrimon, N., & Hsu, J. (2001) · Development · doi:10.1242/dev.128.4.591 · Cited by 64
Isthmus organizer for mesencephalon and metencephalon
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Lao, D.-H., Yusoff, P., Chandramouli, S., Philp, R. J., Fong, C. W., Jackson, R. A., Saw, T. Y., Yu, C. Y., & Guy, G. R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607563200 · Cited by 64
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Gurney, M. E. (2000) · BioEssays · doi:10.1002/(sici)1521-1878(200003)22:3 · Cited by 38
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Strutt, H. L., & Strutt, D. I. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00545-1 · Cited by 61
Tsao, C.-J. (2012) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2012.910 · Cited by 60
Ozaki, K., Miyazaki, S., Tanimura, S., & Kohno, M. (2005) · Journal of Cell Science · doi:10.1242/jcs.02711 · Cited by 60
Control of EGF Receptor Signalling: Lessons from Fruitflies
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Lorenzo, C., & McCormick, F. P. (2020) · Genes & Development · doi:10.1101/gad.341222.120 · Cited by 59
Chambers, D., Medhurst, A. D., Walsh, F. S., Price, J., & Mason, I. J. (2000) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.1999.0801 · Cited by 58
Jin, M.-H., Sawamoto, K., Ito, M., & Okano, H. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.6.2098-2107.2000 · Cited by 57
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The Sevenless signaling pathway: variations of a common theme
Raabe, T. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(00)00020-3 · Cited by 57
Li, X., Brunton, V. G., Burgar, H. R., Wheldon, L. M., & Heath, J. K. (2004) · Journal of Cell Science · doi:10.1242/jcs.01519 · Cited by 57
Mechanisms of FGF gradient formation during embryogenesis
Balasubramanian, R., & Zhang, X. (2016) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2015.10.004 · Cited by 56
Li, W. X. (2005) · Developmental Dynamics · doi:10.1002/dvdy.20295 · Cited by 56
Sugiura, K., Su, Y., Li, Q., Wigglesworth, K., Matzuk, M. M., & Eppig, J. J. (2009) · Biology of Reproduction · doi:10.1095/biolreprod.109.078485 · Cited by 55
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Wang, L., Lee, A. S., Wigg, J. P., Peshavariya, H., Liu, P., & Zhang, H. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17060895 · Cited by 55
Keeping the Receptor Tyrosine Kinase Signaling Pathway in Check: Lessons from Drosophila
Rebay, I. (2002) · Developmental Biology · doi:10.1006/dbio.2002.0806 · Cited by 55
Fate and function of the ventral ectodermal ridge during mouse tail development
Goldman, D. C., Martin, G. R., & Tam, P. (2000) · Development · doi:10.1242/dev.127.10.2113 · Cited by 55
Genolet, O., Monaco, A. A., Dunkel, I., Boettcher, M., & Schulz, E. G. (2021) · Genome biology · doi:10.1186/s13059-021-02321-2 · Cited by 56
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Metadata
- Authors
- Casci, T., Vinós, J., & Freeman, M.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- Corresponding author
- Freeman, Matthew
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1999-03
- Volume
- 96
- Issue
- 5
- Pages
- 655-665
- ISSN
- 0092-8674 (ISSN-L)
- 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
- 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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