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Titolo:
The carboxyl terminus of B class ephrins constitutes a PDZ domain binding motif
Autore:
Lin, D; Gish, GD; Songyang, Z; Pawson, T;
Indirizzi:
Mt Sinai Hosp, Samuel Lunenfeld Res Inst, Program Mol Biol & Canc, Toronto, Mt Sinai Hosp Toronto ON Canada M5G 1X5 Program Mol Biol & Canc, Toronto, Univ Toronto, Dept Mol & Med Genet, Toronto, ON M5S 1A8, Canada Univ Toronto Toronto ON Canada M5S 1A8 Genet, Toronto, ON M5S 1A8, Canada MIT, Dept Biol, Cambridge, MA 02139 USA MIT Cambridge MA USA 02139MIT, Dept Biol, Cambridge, MA 02139 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 6, volume: 274, anno: 1999,
pagine: 3726 - 3733
SICI:
0021-9258(19990205)274:6<3726:TCTOBC>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
RECEPTOR TYROSINE KINASES; DENSITY PROTEIN PSD-95; EPH-FAMILY; TRANSMEMBRANE LIGANDS; MOLECULAR-CLONING; COMMISSURAL AXONS; K+ CHANNELS; IN-VITRO; NUK; PHOSPHATASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
55
Recensione:
Indirizzi per estratti:
Indirizzo: Pawson, T Mt Sinai Hosp, Samuel Lunenfeld Res Inst, Program Mol Biol & Canc, 600 Univ Mt Sinai Hosp 600 Univ Ave Toronto ON Canada M5G 1X5 c, 600 Univ
Citazione:
D. Lin et al., "The carboxyl terminus of B class ephrins constitutes a PDZ domain binding motif", J BIOL CHEM, 274(6), 1999, pp. 3726-3733

Abstract

Ephrin B proteins function as ligands for B class Eph receptor tyrosine kinases and are postulated to possess an intrinsic signaling function. The sequence at the carboxyl terminus of B-type ephrins contains a putative PDZ binding site, providing a possible mechanism through which transmembrane ephrins might interact with cytoplasmic proteins. To test this notion, a day 10.5 mouse embryonic expression library was screened with a biotinylated peptide corresponding to the carboxyl terminus of ephrin B3. Three of the positive cDNAs encoded polypeptides with multiple PDZ domains, representing fragments of the molecule GRIP, the protein syntenin, and PHIP, a novel PDZ domain-containing protein related to Caenorhabditis elegans PAR-3. In addition, the binding specificities of PDZ domains previously predicted by an oriented library approach (Songyang, Z., Fanning, A. S., Fu, C., Xu, J., Marfatia, S. M., Chishti, A. H., Crompton, A., Chan, A. C., Anderson, J. M., and Cantley, L. C. (1997) Science 275, 73-77) identified the tyrosine phosphatase FAP-1 as a potential binding partner for B ephrins. In vitro studies demonstrated that the fifth PDZ domain of FAP-I and full-length syntenin boundephrin B1 via the carboxyl-terminal motif. Lastly, syntenin and ephrin B1 could be co-immunoprecipitated from transfected COS-1 cells, suggesting that PDZ domain binding of B ephrins can occur in cells. These results indicate that the carboxyl-terminal motif of B ephrins provides a binding site forspecific PDZ domain-containing proteins, which might localize the transmembrane ligands for interactions with Eph receptors or participate in signaling within ephrin B-expressing cells.

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Documento generato il 27/11/20 alle ore 13:29:12