The DOI matches its Crossref record; 36 of the 37 references it cites were found in a registry or an index.
The fourth immunoglobulin domain of the stem cell factor receptor couples ligand binding to signal transduction
Open accessAbstract
Receptor dimerization is ubiquitous to the action of all receptor tyrosine kinases, and in the case of dimeric ligands, such as the stem cell factor (SCF), it was attributed to ligand bivalency. However, by using a dimerization-inhibitory monoclonal antibody to the SCF receptor, we confined a putative dimerization site to the nonstandard fourth immunoglobulin-like domain of the receptor. Deletion of this domain not only abolished ligand-induced dimerization and completely inhibited signal transduction, but also provided insights into the mechanism of the coupling of ligand binding to dimer formation. These results identify an intrinsic receptor dimerization site and suggest that similar sites may exist in other receptors.
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“Both mutations affect the fourth Ig domain of KIT, and mutations in this motif near the dimerization site have been shown to result in accelerated ligand dissociation and reduced downstream signal transduction events (68).”
From Comparative analysis of the domestic cat genome reveals genetic signatures underlying feline biology and domestication (2014) · cites this paper as [68]
Citations
Cites
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Signal Transduction by the Platelet-Derived Growth Factor Receptor
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Vascular endothelial growth factor (VEGF) and its receptors
Neufeld, G., Cohen, T., Gengrinovitch, S., & Gluzman‐Poltorak, Z. (1999) · The FASEB Journal · doi:10.1096/fasebj.13.1.9 · Cited by 3,511
Mechanism of Action and In Vivo Role of Platelet-Derived Growth Factor
Heldin, C., & Westermark, B. (1999) · Physiological Reviews · doi:10.1152/physrev.1999.79.4.1283 · Cited by 2,521
Dimerization of cell surface receptors in signal transduction
Heldin, C.-H. (1995) · Cell · doi:10.1016/0092-8674(95)90404-2 · Cited by 1,634
Tzahar, E., Waterman, H., Chen, X., Levkowitz, G., Karunagaran, D., Lavi, S., Ratzkin, B. J., & Yarden, Y. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.10.5276 · Cited by 1,039
Stem Cell Factor and Hematopoiesis
Broudy, V. C. (1997) · Blood · doi:10.1182/blood.v90.4.1345 · Cited by 876
Metadata
- Authors
- Blechman, J. M., Lev, S., Barg, J., Eisenstein, M., Vaks, B., Vogel, Z., Givol, D., & Yarden, Y.
- Affiliations
- Weizmann Institute of Science (IL)
- Tel Aviv University (IL)
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1995-01
- Volume
- 80
- Issue
- 1
- Pages
- 103-113
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2054154416
- Cited by
- 156
- References
- 37
- Citations by year
- 2025: 2 · 2024: 1 · 2023: 1 · 2021: 1 · 2018: 2 · 2017: 3 · 2016: 1 · 2015: 1 · 2014: 6 · 2013: 5 · 2012: 1
- FWCI
- 6.19
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Cell (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Israel Cancer Research Fund
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- CD117, receptor dimerization, ligand binding, signal transduction, receptor tyrosine kinase, domain deletion
- MeSH terms
- Animals, Antibodies, Monoclonal, Base Sequence, Binding Sites, Cells, Cultured, Enzyme Activation, Humans, Ligands, Models, Molecular, Molecular Sequence Data, Mutation, Proto-Oncogene Proteins, Solubility, Signal Transduction, Receptors, Colony-Stimulating Factor, Hematopoietic Cell Growth Factors, Epitope Mapping, Proto-Oncogene Proteins c-kit, Stem Cell Factor, Receptor Protein-Tyrosine Kinases, Mice
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