Control of cell behaviour by signalling through Eph receptors and ephrins

Current Opinion in Neurobiology

Volumn 10, Issue 3, 2000, Pages 400-408

  Mellitzer, Georg ^a   Xu, Qiling ^a   Wilkinson, David G ^a  

^a NATIONAL INSTITUTE FOR MEDICAL RESEARCH   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

EPHRIN; PROTEIN TYROSINE KINASE;

CELL ADHESION; CELL INTERACTION; GROWTH CONE; PRIORITY JOURNAL; REVIEW; SIGNAL TRANSDUCTION;

EID: 0034130476     PISSN: 09594388     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-4388(00)00095-7     Document Type: Review

References (78)

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44. ••]. The phenotype of EphB2/EphB3 double mutants, together with the expression pattern of these receptors and of ephrinB1, suggests that angiogenesis also involves cell interactions within arteries and veins, and between blood vessels and the surrounding mesenchyme.
45. ••]. Together with the requirement for reciprocal expression of EphB4 and ephrinB2 in blood vessels, this strongly suggest a requirement for bidirectional signalling between arteries and veins.
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60. •], this work is an important step towards understanding how Eph receptors can control adhesion versus de-adhesion responses.
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67. Lin D., Gish G.D., Songyang Z., Pawson T. The carboxyl terminus of B class ephrins constitutes a PDZ domain binding motif. J Biol Chem. 274:1999;3726-3733. A number of PDZ-domain-containing proteins are identified that bind to the carboxyl terminus of ephrinB proteins. This is an important step towards understanding the signal transduction pathways controlled by ephrins.
68. •], this work identifies components that are potentially important in signalling and/or localisation of ephrinB proteins.
69. Hock B., Bohme B., Karn T., Yamamoto T., Kaibuchi K., Holtrich U., Holland S., Pawson T., Rubsamen-Waigmann H., Strebhardt K. PDZ-domain-mediated interaction of the Eph-related receptor tyrosine kinase EphB3 and the ras-binding protein AF6 depends on the kinase activity of the receptor. Proc Natl Acad Sci USA. 95:1998;9779-9784.
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71. ••].
72. ••] these studies show that ephrinA proteins transduce signals that regulate cell adhesion and movement.
73. Davy A., Gale N.W., Murray E.W., Klinghoffer R.A., Soriano P., Feuerstein C., Robbins S.M. Compartmentalized signaling by GPI-anchored ephrin-A5 requires the fyn tyrosine kinase to regulate cellular adhesion. Genes Dev. 13:1999;3125-3135. This study shows that ephrinA protein is localised in membrane rafts and that clustering by Eph receptors leads to phosphorylation of unidentified intracellular proteins in the ephrin-expressing cells. This phosphorylation requires the fyn tyrosine kinase and leads to an upregulation of cell attachment to the extracellular matrix.
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78. ••], this work sets the stage for a detailed genetic dissection of the biochemistry and function of Eph receptor-ephrin signalling.