Publication Date:
1994-11-04
Description:
The EPH-related transmembrane tyrosine kinases constitute the largest known family of receptor-like tyrosine kinases, with many members displaying specific patterns of expression in the developing and adult nervous system. A family of cell surface-bound ligands exhibiting distinct, but overlapping, specificities for these EPH-related kinases was identified. These ligands were unable to act as conventional soluble factors. However, they did function when presented in membrane-bound form, suggesting that they require direct cell-to-cell contact to activate their receptors. Membrane attachment may serve to facilitate ligand dimerization or aggregation, because antibody-mediated clustering activated previously inactive soluble forms of these ligands.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, S -- Gale, N W -- Aldrich, T H -- Maisonpierre, P C -- Lhotak, V -- Pawson, T -- Goldfarb, M -- Yancopoulos, G D -- New York, N.Y. -- Science. 1994 Nov 4;266(5186):816-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Regeneron Pharmaceuticals, Tarrytown, NY 10591.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973638" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Animals
;
Cell Line
;
Cell Membrane/*metabolism
;
*DNA-Binding Proteins
;
Ephrin-A1
;
Ephrin-B1
;
Humans
;
Ligands
;
Membrane Proteins/chemistry/*metabolism
;
Molecular Sequence Data
;
Neurons/metabolism
;
Phosphorylation
;
Proteins/chemistry/*metabolism
;
*Proto-Oncogene Proteins
;
Receptor Protein-Tyrosine Kinases/*metabolism
;
*Receptor, EphA5
;
Recombinant Fusion Proteins/metabolism
;
Retroviridae Proteins, Oncogenic/*metabolism
;
Solubility
;
*Transcription Factors
;
Transfection
;
Tumor Cells, Cultured
;
ets-Domain Protein Elk-1
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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