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J Biol Chem, Vol. 275, Issue 18, 13793-13801, May 5, 2000
From the Department of Molecular and Structural Biology, Kyushu
University Graduate School of Medical Science, 3-1-1 Maidashi,
Higashi-ku, Fukuoka 812-8582, Japan
The superoxide-producing phagocyte NADPH oxidase
can be activated by arachidonic acid (AA) or by phosphorylation of
p47phox under cell-free conditions. The
molecular mechanism underlying the activation, however, has remained
largely unknown. Here we demonstrate that AA, at high concentrations
(50-100 µM), induces direct interaction between the
oxidase factors p47phox and
p22phox in parallel with superoxide production.
The interaction, being required for the oxidase activation, is mediated
via the Src homology 3 (SH3) domains of p47phox
(p47-(SH3)2), which are intramolecularly masked in a
resting state. We also show that AA disrupts complexation of
p47-(SH3)2 with its intramolecular target fragment (amino
acids 286-340) without affecting association of p47-(SH3)2
with p22phox, indicating that the disruption
plays a crucial role in the induced interaction with
p22phox. Phosphorylation of
p47phox by protein kinase C partially replaces
the effects of AA; treatment of the SH3 target fragment with PKC
in vitro results in a completely impaired interaction with
p47-(SH3)2, and the same treatment of the full-length
p47phox leads to both interaction with
p22phox and oxidase activation without AA, but
to a lesser extent. Furthermore, phosphorylated
p47phox effectively binds to
p22phox and activates the oxidase in the
presence of AA at low concentrations (1-5 µM), where an
unphosphorylated protein only slightly supports superoxide production.
Thus AA, at high concentrations, fully induces the interaction of
p47phox with p22phox by
itself, whereas, at low concentrations, AA synergizes with phosphorylation of p47phox to facilitate the
interaction, thereby activating the NADPH oxidase.
To whom correspondence should be addressed. Tel.: 81-92-642-6213;
Fax: 81-92-642-6215; E-mail:
hsumi@mailserver.med.kyushu-u.ac.jp.
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