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(Received for publication, May 3, 1995; and in revised form, June 27, 1995) 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.
Volume 270,
Number 35,
Issue of September 01, pp. 20660-20667, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
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