Sequential phosphorylation of protein band 3 by Syk and Lyn tyrosine kinases in intact human erythrocytes: identification of primary and secondary phosphorylation sites.

Détails

ID Serval
serval:BIB_97A1DDD703AE
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Sequential phosphorylation of protein band 3 by Syk and Lyn tyrosine kinases in intact human erythrocytes: identification of primary and secondary phosphorylation sites.
Périodique
Blood
Auteur(s)
Brunati A.M., Bordin L., Clari G., James P., Quadroni M., Baritono E., Pinna L.A., Donella-Deana A.
ISSN
0006-4971
Statut éditorial
Publié
Date de publication
08/2000
Peer-reviewed
Oui
Volume
96
Numéro
4
Pages
1550-1557
Langue
anglais
Résumé
Treatment of intact human erythrocytes with pervanadate induces Tyr (Y)-phosphorylation of the transmembrane protein band 3; in parallel, the activity of the immunoprecipitated tyrosine kinases Syk and Lyn is increased. When erythrocytes are incubated with pervanadate together with PP1, a specific inhibitor of Src kinases, including Lyn, the Y-phosphorylation of band 3 is only partially reduced. Indeed, the PP1-resistant phosphorylation of band 3 precedes and is a prerequisite for its coimmunoprecipitation with Lyn, which interacts with the phosphoprotein via the SH2 domain of the enzyme, as proven by binding competition experiments. Upon recruitment to primarily phosphorylated band 3, Lyn catalyzes the secondary phosphorylation of the transmembrane protein. These data are consistent with the view that band 3 is phosphorylated in intact erythrocytes by both PP1-resistant (most likely Syk) and PP1-inhibited (most likely Lyn) tyrosine kinases according to a sequential phosphorylation process. Similar radiolabeled peptide maps are obtained by tryptic digestion of (32)P-band 3 isolated from either pervanadate-treated erythrocytes or red cell membranes incubated with exogenous Syk and Lyn. It has also been demonstrated by means of mass spectrometry that the primary phosphorylation of band 3 occurs at Y8 and Y21, while the secondary phosphorylation affects Y359 and Y904. (Blood. 2000;96:1550-1557)
Mots-clé
Anion Exchange Protein 1, Erythrocyte, Binding Sites, Enzyme Precursors, Erythrocytes, Humans, Intracellular Signaling Peptides and Proteins, Phosphorylation, Protein-Tyrosine Kinases, Substrate Specificity, src-Family Kinases
Pubmed
Web of science
Création de la notice
24/01/2008 15:46
Dernière modification de la notice
20/08/2019 14:59
Données d'usage