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J. Biol. Chem., Vol. 278, Issue 11, 9019-9026, March 14, 2003
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From the Cardiovascular Research Institute, Department of Cell
Biology and Molecular Medicine and Department of Medicine, University
of Medicine and Dentistry of New Jersey, New Jersey Medical School,
Newark, New Jersey 07103
Although tyrosine kinases are critically involved
in the angiotensin II (Ang II) type 1 (AT1) receptor signaling, how AT1 receptors activate tyrosine kinases is not fully understood. We examined the structural requirements of the AT1 receptor for
transactivation of the epidermal growth factor (EGF) receptor (EGFR).
Studies using carboxyl terminal-truncated AT1 receptors indicated that the amino acid sequence between 312 and 337 is required for activation of EGFR. The role of the conserved YIPP motif in this sequence in
transactivation of EGFR was investigated by mutating tyrosine 319. Ang
II failed to activate EGFR in cells expressing AT1-Y319F, whereas EGFR
was activated even without Ang II in cells expressing AT1-Y319E, which
mimics the AT1 receptor phosphorylated at Tyr-319. Immunoblot analyses
using anti-phospho Tyr-319-specific antibody showed that Ang II
increased phosphorylation of Tyr-319. EGFR interacted with the AT1
receptor but not with AT1-Y319F in response to Ang II stimulation,
whereas the EGFR-AT1 receptor interaction was inhibited in the presence
of dominant negative SHP-2. The requirement of Tyr-319 seems specific
for EGFR because Ang II-induced activation of other tyrosine kinases,
including Src and JAK2, was preserved in cells expressing AT1-Y319F.
Extracellular signal-regulated kinase activation was also maintained in
AT1-Y319F through activation of Src. Overexpression of wild type AT1
receptor in cardiac fibroblasts enhanced Ang II-induced proliferation.
By contrast, overexpression of AT1-Y319F failed to enhance cell
proliferation. In summary, Tyr-319 of the AT1 receptor is
phosphorylated in response to Ang II and plays a key role in mediating
Ang II-induced transactivation of EGFR and cell proliferation, possibly
through its interaction with SHP-2 and EGFR.
Phosphorylation of Tyrosine 319 of the Angiotensin II Type 1 Receptor Mediates Angiotensin II-induced Trans-activation of the
Epidermal Growth Factor Receptor*
*
This work was supported by National Institutes of Health
Grants HL 67724 and HL67727 (to J. S.), American Heart Association Grants 9950673N (to J. S.) and 0230230N (to K. S.), and American Heart Association, Pennsylvania-Delaware Affiliate Fellowship 0020270U
(to K. S.).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.
To whom correspondence should be addressed: Cardiovascular
Research Institute, University of Medicine and Dentistry of New Jersey,
New Jersey Medical School, 185 South Orange Ave., MSB G-609,
Newark, NJ 07103. Tel.: 973-972-8619; Fax: 973-972-8919; E-mail:
Sadoshju@umdnj.edu.
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