Sprouty, an intracellular inhibitor of Ras signaling

Casci, Tanita; Vinós, Javier; Freeman, Matthew

doi:10.1016/s0092-8674(00)80576-0

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

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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Four of the validated miR-21 target genes are known negative regulators of the Ras/MEK/ERK pathway: Spry1, Spry2, Btg2, and Pdcd4.
“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
The Discussion identifies Drosophila Sprouty as an inhibitor of Ras/MAP kinase signaling. The paper predicts that mammalian Sprouty homologs may have the same function, but does not establish it for Spry1 or Spry2 specifically. It does not address Btg2, Pdcd4, or whether these genes are validated miR-21 targets. (LLM, conf=0.88)
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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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