Nuclear Signaling by Receptor Tyrosine Kinases: The First Robin of Spring
Open accessAbstract
The role of receptor tyrosine kinases (RTKs) in transmembrane signaling is well established. Recently, ligand-dependent translocation of RTKs to the nucleus has been reported, but the functional importance of this process remains unclear. In this issue, Sardi et al. (2006) provide evidence for direct signaling in the nucleus by an intracellular ErbB4 receptor fragment that is released upon receptor activation by ligand. The fragment forms a complex with the adaptor TAB2 and the corepressor N-CoR and transits to the nucleus, where it represses transcription of genes that promote the formation of astrocytes.
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Overexpression or increased activity of wild-type EGFR protein can lead to cell proliferation, migration, survival, and anti-apoptosis through signaling cascades, which are strongly associated with the occurrence and development of many cancers such as NSCLC, breast cancer, glioma, head and neck cancer, cervical cancer, and bladder cancer.
“Overexpression or increased activity of wild-type EGFR protein can lead to cell proliferation, migration, survival, and anti-apoptosis through signaling cascades, which are strongly associated with the occurrence and development of many cancers, such as NSCLC, breast cancer, glioma, head and neck cancer, cervical cancer, and bladder cancer.105–108”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [105]
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- Authors
- Schlessinger, J., & Lemmon, M. A.
- Affiliations
- Yale University (US)
- University of Pennsylvania (US)
- Corresponding author
- Schlessinger, Joseph
- Lemmon, Mark A.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2006-10
- Volume
- 127
- Issue
- 1
- Pages
- 45-48
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2034515307
- Cited by
- 98
- References
- 19
- Citations by year
- 2026: 3 · 2025: 1 · 2024: 4 · 2023: 2 · 2022: 5 · 2021: 1 · 2020: 4 · 2019: 5 · 2018: 3 · 2017: 6 · 2016: 1 · 2015: 3 · 2014: 5 · 2013: 5 · 2012: 4
- FWCI
- 5.37
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 2481 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- South Australian Research and Development Institute
- National Cancer Institute (R01CA079992, R01CA096768)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01AR051448, R01-AR051889)
- Topics
- Health Sciences › Medicine › Oncology › HER2/EGFR in Cancer Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Keywords
- receptor tyrosine kinase, nuclear signaling, ErbB4, TAB2, NCoR, transcriptional repression, astrocyte differentiation, corepressors
- MeSH terms
- Animals, Cell Membrane, Cell Nucleus, Gene Expression Regulation, Humans, Ligands, Neurons, Nuclear Proteins, Peptide Fragments, Repressor Proteins, Transcription, Genetic, Signal Transduction, Receptor Protein-Tyrosine Kinases, Intercellular Signaling Peptides and Proteins, Adaptor Proteins, Signal Transducing, Nuclear Receptor Co-Repressor 1, ErbB Receptors, Receptor, ErbB-4
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