ArticleMolecular and cellular biology1998
Activation of Neu (ErbB-2) mediated by disulfide bond-induced dimerization reveals a receptor tyrosine kinase dimer interface.
Article in Molecular and cellular biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 100 citations in OpenAlex.
- Does the ERBB/EGF Signaling Network Serve as a Nexus for Oncogenic Signals in Uveal Melanoma?Biomolecules · 2026Review
- Elucidating activation and deactivation dynamics of VEGFR-2 transmembrane domain with coarse-grained molecular dynamics simulations.PloS one · 2023Article
- The Yin and Yang of ERBB4: Tumor Suppressor and Oncoprotein.Pharmacological reviews · 2022Review
- Article
- HER2 splice variants in breast cancer: investigating their impact on diagnosis and treatment outcomes.Oncotarget · 2020Review
- Membrane receptor activation mechanisms and transmembrane peptide tools to elucidate them.The Journal of biological chemistry · 2020Review
- Modulation of FLT3 signal transduction through cytoplasmic cysteine residues indicates the potential for redox regulation.Redox biology · 2020Article
- The Under-Appreciated Promiscuity of the Epidermal Growth Factor Receptor Family.Frontiers in cell and developmental biology · 2016Review
- Activation of transmembrane cell-surface receptors via a common mechanism? The "rotation model".BioEssays : news and reviews in molecular, cellular and developmental biology · 2015Review
- Normal activation of discoidin domain receptor 1 mutants with disulfide cross-links, insertions, or deletions in the extracellular juxtamembrane region: mechanistic implications.The Journal of biological chemistry · 2014Article
- TACE activation by MAPK-mediated regulation of cell surface dimerization and TIMP3 association.Science signaling · 2012Article
- Vascular endothelial growth factor A competitively inhibits platelet-derived growth factor (PDGF)-dependent activation of PDGF receptor and subsequent signaling events and cellular responses.Molecular and cellular biology · 2012Article
- Oncogenic IL7R gain-of-function mutations in childhood T-cell acute lymphoblastic leukemia.Nature genetics · 2011Article
- Ligand-independent signaling by disulfide-crosslinked dimers of the p75 neurotrophin receptor.Journal of cell science · 2009Article
- Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment.Cell · 2009Article
- Functional selectivity of EGF family peptide growth factors: implications for cancer.Pharmacology & therapeutics · 2009Review
- Suppression of proliferation of two independent NF1 malignant peripheral nerve sheath tumor cell lines by the pan-ErbB inhibitor CI-1033.Cancer biology & therapy · 2008Article
- Mutational activation of ErbB family receptor tyrosine kinases: insights into mechanisms of signal transduction and tumorigenesis.BioEssays : news and reviews in molecular, cellular and developmental biology · 2007Review
- Self-association of the transmembrane domain of RET underlies oncogenic activation by MEN2A mutations.Oncogene · 2006Article
- The epidermal growth factor receptor (EGFR)-S442F mutant displays increased affinity for neuregulin-2beta and agonist-independent coupling with downstream signalling events.The Biochemical journal · 2006Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Receptor dimerization is a crucial intermediate step in activation of signaling by receptor tyrosine kinases (RTKs). However, dimerization of the RTK Neu (also designated ErbB-2, HER-2, and p185(neu)), while necessary, is not sufficient for signaling. Earlier work in our laboratory had shown that introduction of an ectopic cysteine into the Neu juxtamembrane domain induces Neu dimerization but not signaling. Since Neu signaling does require dimerization, we hypothesized that there are additional constraints that govern signaling ability. With the importance of the interreceptor cross-phosphorylation reaction, a likely constraint was the relative geometry of receptors within the dimer. We have tested this possibility by constructing a consecutive series of cysteine substitutions in the Neu juxtamembrane domain in order to force dimerization along a series of interreceptor faces. Within the group that dimerized constitutively, a subset had transforming activity. The substitutions in this subset all mapped to the same face of a predicted alpha helix, the most likely conformation for the intramembrane domain. Furthermore, this face of interaction aligns with the projected Neu* V664E substitution and with a predicted amphipathic interface in the Neu juxtamembrane domain. We propose that these results identify an RTK dimer interface and that dimerization of this RTK induces an extended contact between juxtamembrane and intramembrane alpha helices.
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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.