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Vol. 11, Issue 1, 117-129, January 2000
and§
The LPP gene is the preferred translocation partner
of the HMGIC gene in a subclass of human benign
mesenchymal tumors known as lipomas. Here we have characterized the
LPP gene product that shares 41% of sequence identity
with the focal adhesion protein zyxin. LPP localizes in focal adhesions
as well as in cell-to-cell contacts, and it binds VASP, a protein
implicated in the control of actin organization. In addition, LPP
accumulates in the nucleus of cells upon treatment with leptomycin B,
an inhibitor of the export factor CRM1. The nuclear export of LPP
depends on an N-terminally located leucine-rich sequence that shares
sequence homology with well-defined nuclear export signals. Moreover,
LPP displays transcriptional activation capacity, as measured by
GAL4-based assays. Altogether, these results show that the LPP protein
has multifunctional domains and may serve as a scaffold upon which
distinct protein complexes are assembled in the cytoplasm and in the nucleus.
Laboratory for Molecular Oncology, Center for Human
Genetics, University of Leuven and Flanders Interuniversity Institute
for Biotechnology, B-3000 Leuven, Belgium; and
Laboratoire de Morphogénèse et Signalisation
Cellulaires, Centre National de la Recherche Scientifique, Unité
Mixte de Recherche 144, Institut Curie, Paris 75248, Cedex 05 France
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