Identification of Lck-binding elements in tip of herpesvirus saimiri.

Détails

ID Serval
serval:BIB_CBAAF7423BAF
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Identification of Lck-binding elements in tip of herpesvirus saimiri.
Périodique
Journal of Biological Chemistry
Auteur(s)
Jung J.U., Lang S.M., Friedrich U., Jun T., Roberts T.M., Desrosiers R.C., Biesinger B.
ISSN
0021-9258
Statut éditorial
Publié
Date de publication
1995
Peer-reviewed
Oui
Volume
270
Numéro
35
Pages
20660-20667
Langue
anglais
Résumé
A protein called Tip (tyrosine kinase interacting protein) of herpesvirus saimiri associates with Lck in virus-transformed human T cells and is an in vitro substrate for Lck kinase. Mutational analyses of a GST-Tip fusion protein revealed that binding to Lck requires putative SH3 binding sequences and a sequence homologous to the carboxyl terminus of Src-related kinases. These sequences are referred to as SH3-Binding (SH3B) and C-terminal Src-related Kinase Homology (CSKH) elements. Peptide fragments as short as 37 amino acids containing both SH3B and CSKH elements were sufficient to form a stable complex with Lck in vitro. Furthermore, these same sequences of Tip were necessary for in vivo association with Lck when Tip and Lck were expressed transiently in COS-1 cells or stably in Rat-1 cell lines. These results demonstrate that the CSKH element of Tip participates in the binding of sequences within Lck. Tip of herpesvirus saimiri has apparently acquired such CSKH and SH3B elements for the purpose of targeting cellular protein kinases. The interaction of Tip with Lck may influence Lck kinase activity or its binding to other cellular proteins and thereby alter Lck function in T cells infected by h. saimiri.
Mots-clé
Amino Acid Sequence, Animals, Base Sequence, Binding Sites, Cell Line, Cercopithecus aethiops, DNA Primers, Herpesvirus 2, Saimiriine/metabolism, Lymphocyte Specific Protein Tyrosine Kinase p56(lck), Molecular Sequence Data, Mutagenesis, Site-Directed, Peptide Fragments/chemistry, Peptide Fragments/isolation & purification, Phosphoproteins/isolation & purification, Phosphoproteins/metabolism, Phosphoserine/analysis, Phosphothreonine/analysis, Phosphotyrosine, Point Mutation, Polymerase Chain Reaction, Protein-Tyrosine Kinases/isolation & purification, Protein-Tyrosine Kinases/metabolism, Rats, Recombinant Proteins/isolation & purification, Recombinant Proteins/metabolism, Sequence Homology, Amino Acid, Spodoptera, Structure-Activity Relationship, Transfection, Tyrosine/analogs & derivatives, Tyrosine/analysis, Viral Proteins/isolation & purification, Viral Proteins/metabolism
Pubmed
Web of science
Création de la notice
08/10/2008 11:04
Dernière modification de la notice
03/03/2018 21:27
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