ArticleMolecular and cellular biology2009
The hnRNA-binding proteins hnRNP L and PTB are required for efficient translation of the Cat-1 arginine/lysine transporter mRNA during amino acid starvation.
Article in Molecular and cellular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 83 citations in OpenAlex.
- Transcriptomic Profiling Reveals Lysine-Mediated Proliferative Mechanisms in Mongolian Horse Myogenic Satellite Cells.Animals : an open access journal from MDPI · 2025Article
- Review
- hnRNPL expression dynamics in the embryo and placenta.Gene expression patterns : GEP · 2023Article
- Factors Influencing Proteolysis and Protein Utilization in the Intestine of Pigs: A Review.Animals : an open access journal from MDPI · 2021Review
- The RNA-binding protein PTBP1 promotes ATPase-dependent dissociation of the RNA helicase UPF1 to protect transcripts from nonsense-mediated mRNA decay.The Journal of biological chemistry · 2020Article
- Heterogeneous Nuclear Ribonucleoprotein L Negatively Regulates Foot-and-Mouth Disease Virus Replication through Inhibition of Viral RNA Synthesis by Interacting with the Internal Ribosome Entry Site in the 5' Untranslated Region.Journal of virology · 2020Article
- Mining the Prognostic Value of HNRNPAB and Its Function in Breast Carcinoma.International journal of genomics · 2020Article
- Aberrant expression and regulatory network of splicing factor-SRSF3 in tumors.Journal of Cancer · 2020Review
- Extra dietary protein-bound or free amino acids differently affect the serum concentrations of free amino acids in heat-stressed pigs1.Journal of animal science · 2019Article
- IRES Trans-Acting Factors, Key Actors of the Stress Response.International journal of molecular sciences · 2019Review
- Inclusion of hnRNP L Alternative Exon 7 Is Associated with Good Prognosis and Inhibited by Oncogene SRSF3 in Head and Neck Squamous Cell Carcinoma.BioMed research international · 2019Article
- Translation acrobatics: how cancer cells exploit alternate modes of translational initiation.EMBO reports · 2018Review
- Functional 5' UTR mRNA structures in eukaryotic translation regulation and how to find them.Nature reviews. Molecular cell biology · 2018Review
- Coordinated transcriptional control of adipocyte triglyceride lipase (The Journal of biological chemistry · 2017Article
- Sequence features of viral and human Internal Ribosome Entry Sites predictive of their activity.PLoS computational biology · 2017Article
- Heterogeneous nuclear ribonucleoprotein (hnRNP) L promotes DNA damage-induced cell apoptosis by enhancing the translation of p53.Oncotarget · 2017Article
- Interplay between miR-574-3p and hnRNP L regulates VEGFA mRNA translation and tumorigenesis.Nucleic acids research · 2017Article
- Genome-wide CRISPR screen identifies HNRNPL as a prostate cancer dependency regulating RNA splicing.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- More than just scanning: the importance of cap-independent mRNA translation initiation for cellular stress response and cancer.Cellular and molecular life sciences : CMLS · 2017Review
- HnRNP-L promotes prostate cancer progression by enhancing cell cycling and inhibiting apoptosis.Oncotarget · 2017Article
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
The response to amino acid starvation involves the global decrease of protein synthesis and an increase in the translation of some mRNAs that contain an internal ribosome entry site (IRES). It was previously shown that translation of the mRNA for the arginine/lysine amino acid transporter Cat-1 increases during amino acid starvation via a mechanism that utilizes an IRES in the 5' untranslated region of the Cat-1 mRNA. It is shown here that polypyrimidine tract binding protein (PTB) and an hnRNA binding protein, heterogeneous nuclear ribonucleoprotein L (hnRNP L), promote the efficient translation of Cat-1 mRNA during amino acid starvation. Association of both proteins with Cat-1 mRNA increased during starvation with kinetics that paralleled that of IRES activation, although the levels and subcellular distribution of the proteins were unchanged. The sequence CUUUCU within the Cat-1 IRES was important for PTB binding and for the induction of translation during amino acid starvation. Binding of hnRNP L to the IRES or the Cat-1 mRNA in vivo was independent of PTB binding but was not sufficient to increase IRES activity or Cat-1 mRNA translation during amino acid starvation. In contrast, binding of PTB to the Cat-1 mRNA in vivo required hnRNP L. A wider role of hnRNP L in mRNA translation was suggested by the decrease of global protein synthesis in cells with reduced hnRNP L levels. It is proposed that PTB and hnRNP L are positive regulators of Cat-1 mRNA translation via the IRES under stress conditions that cause a global decrease of protein synthesis.
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