ArticleBlood2005
Rapid ubiquitination of Syk following GPVI activation in platelets.
Article in Blood, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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.
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Who cites it
30 citing papers in PubMed, 63 citations in OpenAlex.
- Phosphorylation at Y317 on Syk negatively regulates both ITAM- and hemITAM-mediated signaling and function in platelets.Blood advances · 2025Article
- TULA Proteins in Men, Mice, Hens, and Lice: Welcome to the Family.International journal of molecular sciences · 2023Review
- TULA-Family Regulators of Platelet Activation.International journal of molecular sciences · 2022Review
- Proteomics: A Tool to Study Platelet Function.International journal of molecular sciences · 2021Review
- Feedback Regulation of Syk by Protein Kinase C in Human Platelets.International journal of molecular sciences · 2019Article
- Ascorbic acid improves thrombotic function of platelets during living donor liver transplantation by modulating the function of the E3 ubiquitin ligases c-Cbl and Cbl-b.The Journal of international medical research · 2019Article
- Cbl interacts with multiple E2s in vitro and in cells.PloS one · 2019Article
- Human Platelet Protein Ubiquitylation and Changes following GPVI Activation.Thrombosis and haemostasis · 2019Article
- Impact of Escherichia coli K12 and O18:K1 on human platelets: Differential effects on platelet activation, RNAs and proteins.Scientific reports · 2018Article
- Possible Molecular Targets of Novel Ruthenium Complexes in Antiplatelet Therapy.International journal of molecular sciences · 2018Review
- Network Analysis Identifies Proinflammatory Plasma Cell Polarization for Secretion of ISG15 in Human Autoimmunity.Journal of immunology (Baltimore, Md. : 1950) · 2016Article
- Regulation of Early Steps of GPVI Signal Transduction by Phosphatases: A Systems Biology Approach.PLoS computational biology · 2015Article
- A respiratory chain controlled signal transduction cascade in the mitochondrial intermembrane space mediates hydrogen peroxide signaling.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Autophagy is induced upon platelet activation and is essential for hemostasis and thrombosis.Blood · 2015Article
- MALT1-ubiquitination triggers non-genomic NF-κB/IKK signaling upon platelet activation.PloS one · 2015Article
- Global proteome analysis identifies active immunoproteasome subunits in human platelets.Molecular & cellular proteomics : MCP · 2014Article
- Dissection of autophagy in human platelets.Autophagy · 2014Article
- Proteasome proteolysis supports stimulated platelet function and thrombosis.Arteriosclerosis, thrombosis, and vascular biology · 2014Article
- Protein degradation systems in platelets.Thrombosis and haemostasis · 2013Review
- Tyrosine phosphorylation on spleen tyrosine kinase (Syk) is differentially regulated in human and murine platelets by protein kinase C isoforms.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Spleen tyrosine kinase (Syk) activation is a key intermediate step in the activation of platelets by the physiologic agonist collagen. We have found that Syk is rapidly ubiquitinated upon activation of platelets by collagen, collagen-related peptide (CRP), and convulxin. The Src family kinase inhibitors prevented Syk phosphorylation and its ubiquitination, indicating that the process is downstream of Src kinases. The ubiquitination of Syk did not cause degradation of the protein as evidenced by the lack of effect of proteasomal and lysosomal inhibitors. We separated ubiquitinated Syk from its nonubiquitinated counterpart and used an in vitro kinase assay to compare their activities. We found that the ubiquitinated Syk appeared to be about 5-fold more active. Using a phosphospecific antibody to Syk (Tyr525/Tyr526) that measures activated Syk, we found that most (60%-75%) of the active Syk is in the ubiquitinated fraction. This result explains the apparent high specific activity of ubiquitinated Syk. In c-Cbl-deficient mice, Syk is not ubiquitinated, implicating c-Cbl as the E3 ligase involved in Syk ubiquitination. Furthermore, Syk is not dephosphorylated in these mice. We propose that c-Cbl plays a regulatory role in glycoprotein VI (GPVI)/Fc receptor gamma (FcRgamma)-chain-dependent platelet activation through its interaction with Syk.
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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 OpenQuestion graph.