ArticleMolecular and cellular biology2007
Deciphering the cross talk between hnRNP K and c-Src: the c-Src activation domain in hnRNP K is distinct from a second interaction site.
Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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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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Who cites it
21 citing papers in PubMed, 37 citations in OpenAlex.
- Heterogeneous nuclear ribonucleoprotein K promotes cap-independent translation initiation of retroviral mRNAs.Nucleic acids research · 2024Article
- Discovery of lipid-mediated protein-protein interactions in living cells using metabolic labeling with photoactivatable clickable probes.Chemical science · 2023Article
- SDCBP-AS1 destabilizes β-catenin by regulating ubiquitination and SUMOylation of hnRNP K to suppress gastric tumorigenicity and metastasis.Cancer communications (London, England) · 2022Article
- Methylated HNRNPK acts on RPS19 to regulate ALOX15 synthesis in erythropoiesis.Nucleic acids research · 2021Article
- Prognostic Value and Immunological Characteristics of a Novel RNA Binding Protein Signature in Cutaneous Melanoma.Frontiers in genetics · 2021Article
- Uncovering the Role of RNA-Binding Protein hnRNP K in B-Cell Lymphomas.Journal of the National Cancer Institute · 2020Article
- Cancer the'RBP'eutics-RNA-binding proteins as therapeutic targets for cancer.Pharmacology & therapeutics · 2019Review
- Review
- RNA-Binding Proteins in the Control of LPS-Induced Macrophage Response.Frontiers in genetics · 2019Review
- Identification of RNA-binding Proteins in Macrophages by Interactome Capture.Molecular & cellular proteomics : MCP · 2016Article
- Translation control of TAK1 mRNA by hnRNP K modulates LPS-induced macrophage activation.RNA (New York, N.Y.) · 2014Article
- Downregulation of hnRNP K by RNAi inhibits growth of human lung carcinoma cells.Oncology letters · 2014Article
- Caspase-3 cleaves hnRNP K in erythroid differentiation.Cell death & disease · 2013Article
- Article
- Direct recruitment of ERK cascade components to inducible genes is regulated by heterogeneous nuclear ribonucleoprotein (hnRNP) K.The Journal of biological chemistry · 2011Article
- Article
- DDX6 recruits translational silenced human reticulocyte 15-lipoxygenase mRNA to RNP granules.RNA (New York, N.Y.) · 2010Article
- Visualization of molecular interactions using bimolecular fluorescence complementation analysis: characteristics of protein fragment complementation.Chemical Society reviews · 2009Review
- Trading translation with RNA-binding proteins.RNA (New York, N.Y.) · 2008Review
- Microplate-based chromatin immunoprecipitation method, Matrix ChIP: a platform to study signaling of complex genomic events.Nucleic acids research · 2008Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The protein tyrosine kinase c-Src is regulated by two intramolecular interactions. The repressed state is achieved through the interaction of the Src homology 2 (SH2) domain with the phosphorylated C-terminal tail and the association of the SH3 domain with a polyproline type II helix formed by the linker region between SH2 and the kinase domain. hnRNP K, the founding member of the KH domain protein family, is involved in chromatin remodeling, regulation of transcription, and translation of specific mRNAs and is a target in different signal transduction pathways. In particular, it functions as a specific activator and a substrate of the tyrosine kinase c-Src. Here we address the question how hnRNP K interacts with and activates c-Src. We define the proline residues in hnRNP K in the proline-rich motifs P2 (amino acids [aa] 285 to 297) and P3 (aa 303 to 318), which are necessary and sufficient for the specific activation of c-Src, and we dissect the amino acid sequence (aa 216 to 226) of hnRNP K that mediates a second interaction with c-Src. Our findings indicate that the interaction with c-Src and the activation of the kinase are separable functions of hnRNP K. hnRNP K acts as a scaffold protein that integrates signaling cascades by facilitating the cross talk between kinases and factors that mediate nucleic acid-directed processes.
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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.