Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands

@article{Holland1996BidirectionalST,
  title={Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands},
  author={Sacha J. Holland and Nicholas W. Gale and Geraldine M. Mbamalu and George D. Yancopoulos and Mark Henkemeyer and Tony Pawson},
  journal={Nature},
  year={1996},
  volume={383},
  pages={722-725}
}
RECEPTOR tyrosine kinases of the EPH class have been implicated in the control of axon guidance and fascieulation1–7, in regulating cell migration8, and in defining compartments in the developing embryo9–11. Efficient activation of EPH receptors generally requires that their ligands be anchored to the cell surface, either through a transmembrane (TM) region or a glycosyl phosphatidylinositol (GPI) group12. These observations have suggested that EPH receptors can transduce signals initiated by… 
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TLDR
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References

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Elk-L3, a novel transmembrane ligand for the Eph family of receptor tyrosine kinases, expressed in embryonic floor plate, roof plate and hindbrain segments.
TLDR
The identification and characterization of the third, and most divergent, member of the transmembrane group of Eph ligands, which is term Elk-L3 (Elk-related receptor ligand number 3), which is notable for its remarkably restricted and prominent expression in the floor plate and roof plate of the developing neural tube and its rhombomere-specificexpression in the developing hindbrain.
Membrane‐bound LERK2 ligand can signal through three different Eph‐related receptor tyrosine kinases.
TLDR
Preliminary mutagenesis of the LERK2 protein suggests a negative regulatory role for its cytoplasmic domain in LerK2 signaling, which is shown to signal through three different Eph‐related receptors, namely Cek5, Cek10 and Elk.
Biological and biochemical activities of a chimeric epidermal growth factor-Elk receptor tyrosine kinase.
TLDR
The Elk cytoplasmic domain is able to induce tyrosine phosphorylation and DNA synthesis in response to an extracellular ligand, suggesting that Elk and related polypeptides function as ligand-dependent receptor tyrosines kinases.
ELF-2, a new member of the Eph ligand family, is segmentally expressed in mouse embryos in the region of the hindbrain and newly forming somites
TLDR
A new member of the Eph ligand family is described, designated ELF-2, which shows closest homology to the other known transmembrane ligand in the family, ELK-L/LERK-2/Cek5-L, with 57% identity in the extracellular domain and striking homology in the cytoplasmic domain.
Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity.
TLDR
A family of cell surface-bound ligands exhibiting distinct, but overlapping, specificities for these EPH-related kinases was identified, suggesting that they require direct cell-to-cell contact to activate their receptors.
Function of the Eph-related kinase rtk1 in patterning of the zebrafish forebrain
TLDR
A dominant-negative approach in the zebrafish embryo is used to interfere with the function of Rtk1, an Eph-related RTK expressed in the developing diencephalon, and it is found that expression of a truncated receptor leads to expansion of the eye field into diencesphalic territory and loss ofdiencephalic structures.
Molecular characterization of a family of ligands for eph‐related tyrosine kinase receptors.
TLDR
Both elk ligand and B61 mRNAs are inducible by tumour necrosis factor in human umbilical vein endothelial cells and both proteins show promiscuity in binding to the elk and the related hek receptors.
Molecular cloning of a ligand for the EPH-related receptor protein-tyrosine kinase Htk.
TLDR
This work localized hematopoietic expression of Htk to the monocytic lineage, suggesting that the ligand may play a role in differentiation and/or proliferation of these cells.
A juxtamembrane autophosphorylation site in the Eph family receptor tyrosine kinase, Sek, mediates high affinity interaction with p59fyn.
TLDR
Two in vitro autophosphorylation sites within the juxtamembrane domain of the Eph family member Sek are identified, and a candidate binding protein for the activated Sek kinase is identified, suggesting signalling through fyn, or fyn-related, tyrosine kinases may be utilised by many members of this large subclass of transmembrane receptors.
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