[HTML][HTML] Prenylation-dependent association of protein-tyrosine phosphatases PRL-1,-2, and-3 with the plasma membrane and the early endosome
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 …
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 …