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J. Biol. Chem., Vol. 275, Issue 28, 21444-21452, July 14, 2000
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From the Institute of Molecular and Cell Biology, 30 Medical Drive,
Singapore 117609, Republic of Singapore
PRL-1, -2, and -3 represent a novel class of
protein-tyrosine phosphatase with a C-terminal prenylation motif.
Although PRL-1 has been suggested to be associated with the nucleus,
the presence of three highly homologous members and the existence of a
prenylation motif call for a more detailed examination of their
subcellular localization. In the present study, we first demonstrate
that mouse PRL-1, -2, and -3 are indeed prenylated. Examination of N-terminal epitope-tagged PRL-1, -2, and -3 expressed in transiently transfected cells suggests that PRL-1, -2, and -3 are present on the
plasma membrane and intracellular punctate structures. Stable Chinese
hamster ovary cells expressing PRL-1 and -3 in an inducible manner were
established. When cells were treated with brefeldin A, PRL-1 and -3 accumulated in a collapsed compact structure around the
microtubule-organizing center. Furthermore, PRL-1 and -3 redistributed
into swollen vacuole-like structures when cells were treated with
wortmannin. These characteristics of PRL-1 and -3 are typical for
endosomal proteins. Electron microscope immunogold labeling reveals
that PRL-1 and -3 are indeed associated with the plasma membrane and
the early endosomal compartment. Expression of PRL-3 is detected in the
epithelial cells of the small intestine, where PRL-3 is present in
punctate structures in the cytoplasm. When cells are treated with
FTI-277, a selective farnesyltransferase inhibitor, PRL-1, -2, and -3 shifted into the nucleus. Furthermore, a mutant form of PRL-2 lacking
the C-terminal prenylation signal is associated with the nucleus. These
results establish that the primary association of PRL-1, -2, and -3 with the membrane of the cell surface and the early endosome is
dependent on their prenylation and that nuclear localization of these
proteins may be triggered by a regulatory event that inhibits their prenylation.
Prenylation-dependent Association of Protein-tyrosine
Phosphatases PRL-1, -2, and -3 with the Plasma Membrane and the Early
Endosome*
*
This work was supported by the National Science and
Technology Board of Singapore.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.
To whom correspondence should be addressed: Inst. of Molecular and
Cell Biology, 30 Medical Dr., Singapore 117609, Republic of Singapore.
Tel.: 65-874-3742; Fax: 65-779-1117; E-mail:
mcbcp@imcb.nus.edu.sg.
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