The torso receptor localizes as well as transduces the spatial signal specifying terminal body pattern in Drosophila
Article Abstract:
The torso (tor) protein is a receptor tyrosine kinase that specifies the end portions of the Drosophila body. The failure to accumulate tor protein at one or both poles leads to inappropriate activity of more centrally located receptor. The gene functions that are required for activating tor are the same systems necessary for this ectopic activity, suggesting that inappropriate diffusion of the ligand to more central regions of the body contribute to this failure. Moreover, these results indicate that the receptor plays a role in spatial signal transduction as well as ligand sequestration for correct localization.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
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Crystal structure of the ligand-binding domain of the receptor tyrosine kinase EphB3
Article Abstract:
The extracellular region of Eph receptors comprises firbonectin type III repeats, a conserved globular domain and a cysteine-rich region. The structure of the active ligand-binding domain of the EphB2 murine receptor was determined using ex-ray crystallography, based on the multiple isomorphous replacement (MIR) method. The structure region involved in ligand recognition was found based on the structure, published data and H-I-loop mutagenesis.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
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The SH2/SH3 adaptor Grb4 transduces B-ephrin reverse signals
Article Abstract:
It has been established that the Src-homology-2/Src-homology-3 domain adaptor protein Grb4 binds to the cytoplasmic domain of B ephrins in a phosphotyrosine-dependent way. This work identifies a biochemical pathway in which cytoskeletal regulators are recruited to Eph-ephrin bidirectional signalling complexes.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2001
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