Abstract
The mechanisms by which most receptor protein-tyrosine kinases (RTKs) transmit signals are now well established. Binding of ligand results in the dimerization of receptor monomers followed by transphosphorylation of tyrosine residues within the cytoplasmic domains of the receptors. This tidy picture has, however, some strange characters lurking around the edges. Cases have now been identified in which RTKs lack kinase activity, but, despite being "dead" appear to have roles in signal transduction. Even stranger are the cases in which genes encoding RTKs produce protein products consisting of only a portion of the kinase domain. At least one such "fractured" RTK appears to be involved in signal transduction. Here we describe how these strange molecules might function and discuss the questions associated with their evolution. BioEssays 23:69-76, 2001.
Keywords
Receptor tyrosine kinaseReceptor Protein-Tyrosine KinasesSignal transductionBiologyReceptorCell biologyTyrosine kinaseProtein kinase domainKinaseTyrosineTropomyosin receptor kinase CBiochemistryGenePlatelet-derived growth factor receptor
MeSH Terms
AnimalsEvolutionMolecularHumansProtein-Tyrosine KinasesProto-Oncogene Proteins c-kitReceptor Protein-Tyrosine KinasesReceptorErbB-3ReceptorsCell SurfaceSignal Transduction
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Publication Info
- Year
- 2000
- Type
- review
- Volume
- 23
- Issue
- 1
- Pages
- 69-76
- Citations
- 90
- Access
- Closed
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Cite This
Michael Kroiher,
Michael A. Miller,
Robert E. Steele
(2000).
Deceiving appearances: signaling by “dead” and “fractured” receptor protein-tyrosine kinases.
BioEssays
, 23
(1)
, 69-76.
https://doi.org/10.1002/1521-1878(200101)23:1<69::aid-bies1009>3.0.co;2-k
Identifiers
- DOI
- 10.1002/1521-1878(200101)23:1<69::aid-bies1009>3.0.co;2-k
- PMID
- 11135311