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Vol. 10, Issue 4, 975-986, April 1999
Department of Anatomy and Cell Biology, Gunma University School of
Medicine, Maebashi 371-8511, Japan
Caveolin-1 was discovered as a major substrate for v-Src, but the
effect of its tyrosine phosphorylation has not been known. We generated
a specific antibody (PY14) to caveolin-1 phosphorylated at tyrosine 14 and studied the significance of the modification. By Western blotting
of lysates of v-Src-expressing cells, PY14 recognized not only a
22-kDa band (the position of nonphosphorylated caveolin-1) but bands at
23-24 and 25 kDa. Bands of slower mobility were diminished by
dephosphorylation and were also observed for mutant caveolin-1 lacking
tyrosine 14. By immunofluorescence microscopy, PY14 did not label
normal cells but detected large dots in v-Src-expressing cells.
Immunoelectron microscopy revealed that the dots corresponded to
aggregated caveolae and/or vesicles of various sizes; besides, the
label was observed in intramembrane particle-free areas in the plasma
membrane, which appeared to have been formed by fusion of flattened
caveolae. A positive reaction with PY14 was found in normal cells after
vanadate or pervanadate treatment; it occurred mainly at 22 kDa by
Western blotting and was not seen as large dots by immunofluorescence
microscopy. Detergent solubility, oligomerization, and association with
caveolin-2 were observed similarly for caveolin-1 in normal and
v-Src-expressing cells. The results indicate that phosphorylation of
caveolin-1 in v-Src-expressing cells occurs at multiple residues and
induces flattening, aggregation, and fusion of caveolae and/or
caveolae-derived vesicles.
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