Transmembrane signaling by a chimera of the Escherichia coli aspartate receptor and the human insulin receptor.
AUTOR(ES)
Moe, G R
RESUMO
Since many receptors apparently contain only one or two membrane-spanning segments, their transmembrane topology should be similar. This feature suggests that these receptors share common mechanisms of transmembrane signaling. To test the degree of conservation of signaling properties, a chimeric receptor containing the ligand-binding extracellular domain of the Escherichia coli aspartate chemoreceptor and the cytosolic portion of the human insulin receptor was constructed. This chimeric receptor is active as a tyrosine kinase, and aspartate stimulates its activity. Some interesting differences are noted in the target proteins phosphorylated by the chimera compared to the wild-type insulin receptor. These results indicate that features of the signaling mechanisms used by these diverse receptors are conserved, but that interesting changes in the protein properties are caused by differences in the neighboring domains.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=297694Documentos Relacionados
- Molecular mechanism of transmembrane signaling by the aspartate receptor: a model.
- Linking functional domains of the human insulin receptor with the bacterial aspartate receptor.
- Determination of transmembrane protein structure by disulfide cross-linking: the Escherichia coli Tar receptor.
- Catalysis of serine and tyrosine autophosphorylation by the human insulin receptor.
- Disulfide cross-linking studies of the transmembrane regions of the aspartate sensory receptor of Escherichia coli.