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(Received for publication, February 22, 1996, and in revised form, August 14, 1996)
From the Department of Biochemistry, Institute of Medical Science,
University of Tokyo, Tokyo 108, Japan
Src homology 2 (SH2) domains have been
demonstrated to bind tyrosine-phosphorylated proteins that participate
in signaling by growth factors and oncogenes by recognizing amino acid
sequences containing phosphotyrosine residue. We found that SH2 domains
such as Ash/Grb2, the 85-kDa subunit of phosphatidylinositol
3-kinase, and phospholipase C
Volume 271, Number 44,
Issue of November 1, 1996
pp. 27931-27935
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
-Tubulin Binds Src Homology 2 Domains through a Region
Different from the Tyrosine-phosphorylated Protein-recognizing
Site
1 also bind 
-tubulin through a
different region that recognizes phosphotyrosine in vitro
and in vivo. Furthermore, binding occurs even when
the SH2 domain is occupied by tyrosine-phosphorylated epidermal growth
factor receptors. Using deleted constructs of Ash/Grb2 SH2, we found
that carboxyl-terminal strands E and F, and 
helix B (region
``c'') are required for binding. A synthetic peptide
(FLWVVKFNSLNELVDYH) composed of region c inhibited the binding of
-tubulin to the SH2 domains of Ash/Grb2, phosphatidylinositol
3-kinase, and phospholipase C1. The co-localization of SH2 proteins
and microtubules is also confirmed by immunostaining. These data
suggest that microtubules play important roles in the assembly of
signaling molecules complexes containing SH2 proteins.
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