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Vol. 9, Issue 7, 1661-1674, July 1998
Department of Cell Biology, University of Virginia Health Sciences
Center, Charlottesville, Virginia 22908
Secretory carrier membrane proteins (SCAMPs) are ubiquitously
expressed proteins of post-Golgi vesicles. In the presence of the
tyrosine phosphatase inhibitor vanadate, or after overexpression in
Chinese hamster ovary (CHO) cells, SCAMP1 and SCAMP3 are phosphorylated selectively on tyrosine residue(s). Phosphorylation is reversible after
vanadate washout in situ or when isolated SCAMP3 is incubated with the
recombinant tyrosine phosphatase PTP1B. Vanadate also causes the
partial accumulation of SCAMP3, but not SCAMP1, in "patches" at or
near the cell surface. A search for SCAMP kinase activities has shown
that SCAMPs 1 and 3, but not SCAMP2, are tyrosine phosphorylated in
EGF-stimulated murine fibroblasts overexpressing the EGF receptor
(EGFR). EGF catalyzes the progressive phosphorylation of the SCAMPs up
to 1 h poststimulation and may enhance colocalization of the EGFR
and SCAMP3 within the cell interior. EGF also induces SCAMP-EGFR
association, as detected by coimmunoprecipitation, and phosphorylation
of SCAMP3 is stimulated by the EGFR in vitro. These results suggest
that phosphorylation of SCAMPs, either directly or indirectly, may be
functionally linked to the internalization/down-regulation of the EGFR.
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