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J Biol Chem, Vol. 273, Issue 10, 5765-5770, March 6, 1998
From the Department of Molecular Oncology, Genentech, Inc.,
South San Francisco, California 94080
Wiskott-Aldrich syndrome is an X-linked
hematopoietic disease that manifests itself in platelet deficiency and
a compromised immune system. Analysis of hematopoietic cells from
affected individuals reveals that mutations in the Wiskott-Aldrich
syndrome protein (WASP) result in structural and functional
abnormalities in the cell cortex, consistent with the suggestion that
WASP is involved with regulation of the actin-rich cortical
cytoskeleton. Here we report that WASP interacts with a recently
described cytoskeletal-associated protein, PSTPIP, a molecule that is
related to the Schizosaccharomyces pombe cleavage furrow
regulatory protein, CDC15p. This association is mediated by an
interaction between the PSTPIP SH3 domain and two polyproline-rich
regions in WASP. Co-expression of PSTPIP with WASP in vivo
results in a loss of WASP-induced actin bundling activity and
co-localization of the two proteins, which requires the PSTPIP SH3
domain. Analysis of tyrosine phosphorylation of PSTPIP reveals that two
sites are modified in response to v-Src co-transfection or pervanadate
incubation. One of these tyrosines is found in the SH3 domain
poly-proline recognition site, and mutation of this tyrosine to
aspartate or glutamate to mimic this phosphorylation state results in a
loss of WASP binding in vitro and a dissolution of
co-localization in vivo. In addition, PSTPIP that is
tyrosine phosphorylated in the SH3 domain interacts poorly with WASP
in vitro. These data suggest that the PSTPIP and WASP interaction is regulated by tyrosine phosphorylation of the PSTPIP SH3
domain, and this binding event may control aspects of the actin
cytoskeleton.
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