Extracellular domain of the boss transmembrane ligand acts as an antagonist of the sev receptor
Article Abstract:
The cell-surface proteins sevenless (sev), a tyrosine-kinase receptor, and bride of sevenless (boss), a ligand, are important in inductive interactions between cells. The structure of boss has been shown to contain seven transmembrane segments and a large extracellular domain. The seven transmembrane domain is necessary for its activation of tyrosine phosphorylation of the sev receptor. It has also been shown in vivo and in vitro that in soluble form of boss is an antagonist of the sev receptor.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
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Retinoid-X receptor signalling in the developing spinal cord
Article Abstract:
Gene expression is regulated by retinoids via the action of retinoic acid receptors (RARs) and retinoid-X receptors (RXRs). An assay in transgenic mic based on the expression of a fusion protein linking either RXR or RAR to the yeast Ga14 DNA-binding domain is described. Receptor activation in the spinal cord is detected in a pattern suggesting that the receptor operates in the maturation of limb-innervating motor neurons.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
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Regulation of repulsion versus adhesion by different splice forms of an Eph receptor
Article Abstract:
Research into the impact of different splice forms of Eph tyrosine kinase receptors on cell adhesion and repulsion is presented. The alternative use of different splice forms of a tyrosine kinase receptor can modulate the response between adhesion and repulsion in the development of an embryo.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2000
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