ArticleOncogene2003
Tr-kit promotes the formation of a multimolecular complex composed by Fyn, PLCgamma1 and Sam68.
Article in Oncogene, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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.
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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
29 citing papers in PubMed, 76 citations in OpenAlex.
- A non-catalytic role of IPMK is required for PLCγ1 activation in T cell receptor signaling by stabilizing the PLCγ1-Sam68 complex.Cell communication and signaling : CCS · 2024Article
- Sam68 is a druggable vulnerability point in cancer stem cells.Cancer metastasis reviews · 2024Review
- DNA Damage Regulates the Functions of the RNA Binding Protein Sam68 through ATM-Dependent Phosphorylation.Cancers · 2022Article
- Research progress on RNA-binding proteins in breast cancer.Oncology letters · 2022Review
- Article
- Coordination of RNA Processing Regulation by Signal Transduction Pathways.Biomolecules · 2021Review
- Sam68 splicing regulation contributes to motor unit establishment in the postnatal skeletal muscle.Life science alliance · 2020Article
- Emerging Contribution of PancRNAs in Cancer.Cancers · 2020Review
- Leptin, Adiponectin, and Sam68 in Bone Metastasis from Breast Cancer.International journal of molecular sciences · 2020Review
- The Role of RNA Splicing Factors in Cancer: Regulation of Viral and Human Gene Expression in Human Papillomavirus-Related Cervical Cancer.Frontiers in cell and developmental biology · 2020Review
- Tr-KIT/c-KIT ratio in renal cell carcinoma.Molecular biology reports · 2019Article
- The stem cell factor (SCF)/c-KIT signalling in testis and prostate cancer.Journal of cell communication and signaling · 2017Article
- SAM68: Signal Transduction and RNA Metabolism in Human Cancer.BioMed research international · 2015Review
- High expression level and nuclear localization of Sam68 are associated with progression and poor prognosis in colorectal cancer.BMC gastroenterology · 2013Article
- Protein-tyrosine kinase signaling in the biological functions associated with sperm.Journal of signal transduction · 2012Article
- Met receptors induce Sam68-dependent cell migration by activation of alternate extracellular signal-regulated kinase family members.The Journal of biological chemistry · 2011Article
- Genotoxic stress causes the accumulation of the splicing regulator Sam68 in nuclear foci of transcriptionally active chromatin.Nucleic acids research · 2010Article
- The splicing regulator Sam68 binds to a novel exonic splicing silencer and functions in SMN2 alternative splicing in spinal muscular atrophy.The EMBO journal · 2010Article
- Alternative splicing modulates autoinhibition and SH3 accessibility in the Src kinase Fyn.Molecular and cellular biology · 2009Article
- Sam68 regulates a set of alternatively spliced exons during neurogenesis.Molecular and cellular biology · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tr-kit is a truncated form of the tyrosine kinase receptor c-kit expressed in the haploid phase of spermatogenesis. Upon microinjection, tr-kit triggers metaphase-to-anaphase transition in mouse eggs by the sequential activation of Fyn and PLCgamma1. Here, we show that tr-kit promotes the interaction of several tyrosine-phosphorylated proteins with the SH3 domain of PLCgamma1. Western blot analysis indicates that one of these proteins is Sam68, an RNA-binding protein that is known to interact with and be phosphorylated by Src-like kinases in mitosis. tr-kit promotes the association of Sam68 with PLCgamma1 and Fyn in a multimolecular complex, as demonstrated by co-immunoprecipitation of the phosphorylated forms of these proteins using antibodies directed to anyone of the partners of the complex. Expression of tr-kit potentiates the interaction of endogenous Sam68 also with the SH3 domain of Fyn. Furthermore, the subcellular localization of Sam68 is affected by tr-kit through activation of Fyn in live cells. Lastly, we show that interaction with the SH3 domain of Fyn triggers the release of Sam68 from bound RNA. Thus, our data suggest that tr-kit promotes the formation of a multimolecular complex composed of Fyn, PLCgamma1 and Sam68, which allows phosphorylation of PLCgamma1 by Fyn, and may modulate RNA metabolism.
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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.