Eph receptors and ephrins Journal Article


Authors: Himanen, J. P.; Nikolov, D. B.
Article Title: Eph receptors and ephrins
Abstract: Eph receptors, the largest subfamily of receptor tyrosine kinases (RTKs), and their ephrin ligands are important mediators of cell-cell communication regulating cell attachment, shape, and mobility. Eph signaling is crucial for the development of many tissues and organs including the nervous and cardiovascular systems. Both Ephs and ephrins are membrane-bound and their interactions at sites of cell-cell contact initiate unique bi-directional signaling cascades where information is transduced in both the receptor- and the ligand-expressing cells. Recent studies summarized in this review reveal how the signaling process is triggered upon ligand-receptor binding via the formation of a 2:2 circular heterotetramer. This fixes the orientation of the participating molecules and facilitates phosphorylation of their cytoplasmic domains which then interact with downstream signaling factors. The elucidation of the structural details of Eph-ephrin recognition and binding should yield insight into the future development of novel therapeutic agents targeting cardiovascular function, nerve regeneration, and cancer. © 2002 Elsevier Science Ltd. All rights reserved.
Keywords: signal transduction; protein expression; protein phosphorylation; review; nonhuman; animal; metabolism; animals; cell maturation; protein binding; protein tyrosine kinase; angiogenesis; physiology; growth, development and aging; chemistry; regulatory mechanism; cardiovascular system; molecular recognition; nerve fiber; ligand; cytoplasm; development; cell adhesion; cell communication; eph receptors; nerve regeneration; axons; receptors, eph family; ephrin; nervous system; ephrins; axon guidance; ephrin receptor; humans; human; article; cardiovascular function
Journal Title: International Journal of Biochemistry and Cell Biology
Volume: 35
Issue: 2
ISSN: 1357-2725
Publisher: Elsevier Inc.  
Date Published: 2003-02-01
Start Page: 130
End Page: 134
Language: English
DOI: 10.1016/s1357-2725(02)00096-1
PUBMED: 12479863
PROVIDER: scopus
DOI/URL:
Notes: Export Date: 12 September 2014 -- Source: Scopus
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  1. Dimitar B Nikolov
    86 Nikolov
  2. Juha P Himanen
    50 Himanen