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J Biol Chem, Vol. 275, Issue 14, 10604-10610, April 7, 2000
From the We previously demonstrated that
Cooperative Signaling between
6
4
Integrin and ErbB-2 Receptor Is Required to Promote
Phosphatidylinositol 3-Kinase-dependent Invasion*
,,,, and¶
Molecular Oncogenesis Laboratory, Regina
Elena Cancer Institute, Via delle Messi d'Oro, 156-00158 Rome, Italy
and the § Beth Israel Deaconess Medical Center and Harvard
Medical School, Boston, Massachusetts 02215
4 integrin subunit overexpression increases
in vitro invasiveness of NIH3T3 cells that have been
transformed by ErbB-2 oncogene. We used this model to identify domains
within the large 4 cytoplasmic domain that are involved in the interaction of 
64 with ErbB-2,
invasion, and phosphatidylinositol 3-kinase (PI3K) activation. For this
purpose, we expressed deletion mutants of 4 that lacked
either all or portions of the 4 cytoplasmic domain in
NIH3T3/ErbB-2 cells. We also used an ecto-domain mutant in which most
of the extracellular domain of 4 was replaced with a
c-Myc tag. These transfectants were examined for their ability to
invade Matrigel and their ability to activate PI3K, as well as for the
ability of 64 to co-immunoprecipitate
with ErbB-2. The results obtained revealed that a region of the
4 cytoplasmic domain between amino acids 854 and 1183 is
critical for the ability of 64 integrin
to increase invasion. Interestingly, the extracellular domain of
4 is not necessary for 64
to stimulate invasion. The association of
64 with ErbB-2 is dependent upon the
4 cytoplasmic domain and can occur in the absence of
64 heterodimerization. Finally, we
observed strong activation of PI3K with 4 wild type and
with those 4 deletion mutants that were able to
stimulate invasion upon the expression in NIH3T3/ErbB-2 cells. In
conclusion, our results establish that there is cooperation between
64 and ErbB-2 in promoting
PI3K-dependent invasion and implicate a specific region of
the 4 cytoplasmic domain (amino acids 854-1183) in this event.
*
This work was supported by Associazione Italiana Ricerca sul
Cancro.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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