Molecular features underlying the sequential phosphorylation of HS1 protein and its association with c-Fgr protein-tyrosine kinase.

Détails

ID Serval
serval:BIB_54F4BF4646CC
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Molecular features underlying the sequential phosphorylation of HS1 protein and its association with c-Fgr protein-tyrosine kinase.
Périodique
Journal of Biological Chemistry
Auteur⸱e⸱s
Brunati A.M., Donella-Deana A., James P., Quadroni M., Contri A., Marin O., Pinna L.A.
ISSN
0021-9258
Statut éditorial
Publié
Date de publication
03/1999
Peer-reviewed
Oui
Volume
274
Numéro
11
Pages
7557-7564
Langue
anglais
Résumé
The hematopoietic lineage cell-specific protein HS1 was shown to undergo a process of sequential phosphorylation both in vitro and in vivo, which is synergistically mediated by Syk and Src family protein-tyrosine kinases and essential for B cell antigen receptor-mediated apoptosis. We have now identified tyrosine 222 as the HS1 residue phosphorylated by the Src family protein kinases c-Fgr and Lyn, and we show that a truncated form of HS1 (HS1-208-401) lacking the N-terminal putative DNA binding region and the C-terminal Src homology 3 (SH3) domain is still able to undergo all the steps of sequential phosphorylation as efficiently as full-length HS1. We also show that a stable association of phospho-HS1 with c-Fgr through its SH2 domain requires previous autophosphorylation of the kinase and is prevented by subsequent phosphorylation of Tyr-222. Kinetic studies with HS1 and its truncated forms previously phosphorylated by Syk and with a peptide substrate reproducing the sequence around tyrosine 222 support the view that efficient phosphorylation of HS1 by Src family protein kinases entirely relies on TyrP-SH2 domain interaction with negligible, if any, contribution of local specificity determinants. Our data indicate that the proline-rich region of HS1 bordered by tyrosyl residues affected by Syk and Src family kinases represents a functional domain designed to undergo a process of sequential phosphorylation.
Mots-clé
Amino Acid Sequence, Blood Proteins, Enzyme Precursors, Intracellular Signaling Peptides and Proteins, Kinetics, Molecular Sequence Data, Molecular Weight, Peptide Mapping, Phosphorylation, Protein-Tyrosine Kinases, Proto-Oncogene Proteins, Recombinant Proteins, src-Family Kinases
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 15:46
Dernière modification de la notice
20/08/2019 14:09
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