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J. Biol. Chem., Vol. 276, Issue 35, 32875-32882, August 31, 2001

This Article Full Text Full Text (PDF) All Versions of this Article: 276/35/32875    most recent M010400200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Si, X. Articles by Pallen, C. J. Search for Related Content PubMed PubMed Citation Articles by Si, X. Articles by Pallen, C. J. Social Bookmarking                      What's this?

Interaction of Farnesylated PRL-2, a Protein-tyrosine Phosphatase, with the -Subunit of Geranylgeranyltransferase II^*

Xiaoning Si, Qi Zeng, Chee Hoe Ng, Wanjin Hong, and Catherine J. Pallen

From the Institute of Molecular and Cell Biology, 30 Medical Drive, Singapore 117609, Republic of Singapore

Protein of regenerating liver (PRL)-1, -2, and -3 comprise a subgroup of closely related protein-tyrosine phosphatases featuring a C-terminal prenylation motif conforming to either the consensus sequence for farnesylation, CAAX, or geranylgeranylation, CCXX. Yeast two-hybrid screening for PRL-2-interacting proteins identified the -subunit of Rab geranylgeranyltransferase II (GGT II). The specific interaction of GGT II with PRL-2 but not with PRL-1 or -3 occurred in yeast and HeLa cells. Chimeric PRL-1/-2 molecules were tested for their interaction with GGT II, and revealed that the C-terminal region of PRL-2 is required for interaction, possibly the PRL variable region immediately preceeding the CAAX box. Additionally, PRL-2 prenylation is prequisite for GGT II binding. As prenylated PRL-2 is localized to the early endosome, we propose that this is where the interaction occurs. PRL-2 is not a substrate for GGT II, as isoprenoid analysis showed that PRL-2 was solely farnesylated in vivo. Co-expression of the -subunit () of GGT II, GGT II, and PRL-2 resulted in /GGT II heterodimer formation and prevented PRL-2 binding. Expression of PRL-2 alone inhibited the endogenous /GGT II activity in HeLa cells. Together, these results indicate that the binding of GGT II and PRL-2 to GGT II is mutually exclusive, and suggest that PRL-2 may function as a regulator of GGT II activity.

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