ArticleMolecular and cellular biology1990
Epidermal growth factor receptor cytoplasmic domain mutations trigger ligand-independent transformation.
Article in Molecular and cellular biology, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 29 citations in OpenAlex.
- Article
- Molecular mechanism for a role of SHP2 in epidermal growth factor receptor signaling.Molecular and cellular biology · 2003Article
- The molecular basis of viral oncolysis: usurpation of the Ras signaling pathway by reovirus.The EMBO journal · 1998Article
- Dephosphorylation of receptor tyrosine kinases as target of regulation by radiation, oxidants or alkylating agents.The EMBO journal · 1996Article
- The v-erbB oncogene confers enhanced cellular susceptibility to reovirus infection.Journal of virology · 1996Article
- Proliferation and motility responses of primary and recurrent gliomas related to changes in epidermal growth factor receptor expression.Journal of neuro-oncology · 1996Article
- Modulation of erbB kinase activity and oncogenic potential by single point mutations in the glycine loop of the catalytic domain.Molecular and cellular biology · 1994Article
- EGF receptor in neoplasia and metastasis.Cancer metastasis reviews · 1993Review
- Differential effects of carboxy-terminal sequence deletions on platelet-derived growth factor receptor signaling activities and interactions with cellular substrates.Molecular and cellular biology · 1992Article
- Article
- Membrane-anchored form of v-sis/PDGF-B induces mitogenesis without detectable PDGF receptor autophosphorylation.The Journal of cell biology · 1991Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The transforming gene product of avian erythroblastosis virus, v-erbB, is derived from the epidermal growth factor (EGF) receptor but has lost its extracellular ligand-binding domain and was mutated in its cytoplasmic portion, which is thought to be responsible for biological signal generation. We have repaired the deletion of extracellular EGF-binding sequences and investigated the functional consequences of cytoplasmic erbB mutations. Within the resulting EGF receptors, the autophosphorylation activities of the cytoplasmic domains of v-erbB-H and v-erbB-ES4 were fully ligand dependent in intact cells. However, the mitogenic and transforming signaling activities of an EGF receptor carrying v-erbB-ES4 (but not v-erbB-H) cytoplasmic sequences remained ligand independent, whereas those of a receptor with a v-erbB-H cytoplasmic domain were regulated by EGF or transforming growth factor alpha. Thus, structural alterations in the cytoplasmic domain of growth factor receptor tyrosine kinases may induce constitutive signaling activity without autophosphorylation. These findings provide new insight into the mechanism of receptor-mediated signal transduction and suggest a novel alternative for subversion of cellular control mechanisms and proto-oncogene activation.
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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.