ArticleMolecular biology of the cell2004
Tyrosine phosphorylation of Sprouty proteins regulates their ability to inhibit growth factor signaling: a dual feedback loop.
Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 54 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
54 citing papers in PubMed, 124 citations in OpenAlex.
- Targeting exosomes enveloped EBV-miR-BART1-5p-antagomiRs for NPC therapy through both anti-vasculogenic mimicry and anti-angiogenesis.Cancer medicine · 2023Article
- A dominant negative mutation uncovers cooperative control of caudal Wolffian duct development by Sprouty genes.Cellular and molecular life sciences : CMLS · 2022Article
- Sprouty3, but Not Sprouty1, Expression Is Beneficial for the Malignant Potential of Osteosarcoma Cells.International journal of molecular sciences · 2021Article
- Review
- Fibroblast Growth Factor Receptors (FGFRs) and Noncanonical Partners in Cancer Signaling.Cells · 2021Review
- Identification of key features required for efficient S-acylation and plasma membrane targeting of sprouty-2.Journal of cell science · 2020Article
- SPRED proteins and their roles in signal transduction, development, and malignancy.Genes & development · 2020Review
- Exosomal Delivery of AntagomiRs Targeting Viral and Cellular MicroRNAs Synergistically Inhibits Cancer Angiogenesis.Molecular therapy. Nucleic acids · 2020Article
- Sprouty1 Controls Genitourinary Development via its N-Terminal Tyrosine.Journal of the American Society of Nephrology : JASN · 2019Article
- Sprouty2-a Novel Therapeutic Target in the Nervous System?Molecular neurobiology · 2019Review
- Feedback regulation of RTK signaling in development.Developmental biology · 2019Review
- Inhibition of cardiomyocyte Sprouty1 protects from cardiac ischemia-reperfusion injury.Basic research in cardiology · 2019Article
- Negative regulation of lens fiber cell differentiation by RTK antagonists Spry and Spred.Experimental eye research · 2018Article
- Insights into the Proteome of Gastrointestinal Stromal Tumors-Derived Exosomes Reveals New Potential Diagnostic Biomarkers.Molecular & cellular proteomics : MCP · 2018Article
- PKM2 in carcinogenesis and oncotherapy.Oncotarget · 2017Review
- Hypoxia inducible factors regulate the transcription of the sprouty2 gene and expression of the sprouty2 protein.PloS one · 2017Article
- Sprouty2 and -4 hypomorphism promotes neuronal survival and astrocytosis in a mouse model of kainic acid induced neuronal damage.Hippocampus · 2016Article
- Sprouty2 mediated tuning of signalling is essential for somite myogenesis.BMC medical genomics · 2015Article
- Cbl-family ubiquitin ligases and their recruitment of CIN85 are largely dispensable for epidermal growth factor receptor endocytosis.The international journal of biochemistry & cell biology · 2014Article
- The developing story of Sprouty and cancer.Cancer metastasis reviews · 2014Review
Corrections and comments
- Retraction · 2022-06-23Duplication of/in Image · Error in Image · Manipulation of Images · · see also: https://pubpeer.com/publications/CAADE39999964553D2BED04C698EB5
- RetractedRetraction.2022
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Sprouty proteins are recently identified receptor tyrosine kinase (RTK) inhibitors potentially involved in many developmental processes. Here, we report that Sprouty proteins become tyrosine phosphorylated after growth factor treatment. We identified Tyr55 as a key residue for Sprouty2 phosphorylation and showed that phosphorylation was required for Sprouty2 to inhibit RTK signaling, because a mutant Sprouty2 lacking Tyr55 augmented signaling. We found that tyrosine phosphorylation of Sprouty2 affected neither its subcellular localization nor its interaction with Grb2, FRS2/SNT, or other Sprouty proteins. In contrast, Sprouty2 tyrosine phosphorylation was necessary for its binding to the Src homology 2-like domain of c-Cbl after fibroblast growth factor (FGF) stimulation. To determine whether c-Cbl was required for Sprouty2-dependent cellular events, Sprouty2 was introduced into c-Cbl-wild-type and -null fibroblasts. Sprouty2 efficiently inhibited FGF-induced phosphorylation of extracellular signal-regulated kinase 1/2 in c-Cbl-null fibroblasts, thus indicating that the FGF-dependent binding of c-Cbl to Sprouty2 was dispensable for its inhibitory activity. However, c-Cbl mediates polyubiquitylation/proteasomal degradation of Sprouty2 in response to FGF. Last, using Src-family pharmacological inhibitors and dominant-negative Src, we showed that a Src-like kinase was required for tyrosine phosphorylation of Sprouty2 by growth factors. Thus, these data highlight a novel negative and positive regulatory loop that allows for the controlled, homeostatic inhibition of RTK signaling.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.