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J. Biol. Chem., Vol. 275, Issue 38, 29894-29899, September 22, 2000
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From the We previously identified intersectin, a multiple
EH and SH3 domain-containing protein, as a component of the endocytic
machinery. Overexpression of the SH3 domains of intersectin blocks
transferrin receptor endocytosis, possibly by disrupting targeting of
accessory proteins of clathrin-coated pit formation. More recently, we
identified mammalian Sos, a guanine-nucleotide exchange factor for Ras,
as an intersectin SH3 domain-binding partner. We now demonstrate that
overexpression of intersectin's SH3 domains blocks activation of Ras
and MAP kinase in various cell lines. Several studies suggest that activation of MAP kinase downstream of multiple receptor types is
dependent on endocytosis. Thus, the dominant-negative effect of the SH3
domains on Ras/MAP kinase activation may be indirectly mediated through
a block in endocytosis. Consistent with this idea, incubating cells at
4 °C or with phenylarsine oxide, treatments previously established
to inhibit EGF receptor endocytosis, blocks EGF-dependent
activation of MAP kinase. However, under these conditions, Ras activity
is unaffected and overexpression of the SH3 domains of intersectin is
still able to block Ras activation. Thus, intersectin SH3 domain
overexpression can effect EGF-mediated MAP kinase activation directly
through a block in Ras, consistent with a functional role for
intersectin in Ras activation.
Intersectin Can Regulate the Ras/MAP Kinase Pathway Independent
of Its Role in Endocytosis*
,§,
Department of Neurology and Neurosurgery,
Montreal Neurological Institute, McGill University, Montreal,
Quebec H3A 2B4, Canada and the ¶ Laboratory of Signal
Transduction, National Institute of Environmental Health Sciences,
Research Triangle Park, North Carolina 27709
*
This work was supported by a research contract from BioChem
Pharma (Laval, Quebec, Canada) and by Medical Research Council of
Canada Operating Grant MT-13461 (to P. S. M.).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.
A Scholar of the Medical Research Council of Canada. To whom
correspondence should be addressed: Dept. of Neurology and
Neurosurgery, Montreal Neurological Institute, McGill University, 3801 University St., Montreal, Quebec H3A 2B4, Canada. Tel.: 514-398-7355;
Fax: 514-398-8106; E-mail: mcpm@musica.mcgill.ca.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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