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Title: Nuclear speckles and nucleoli targeting by PIP2-PDZ domain interactions
Authors: Mortier, Eva
Wuytens, Gunther
Leenaerts, Iris
Hannes, Femke
Heung, Man Y
Degeest, Gisèle
David, Guido
Zimmermann, Pascale # ×
Issue Date: Jul-2005
Publisher: Nature Publishing Group
Series Title: EMBO Journal vol:24 issue:14 pages:2556-2565
Abstract: PDZ (Postsynaptic density protein, Disc large, Zona occludens) domains are protein-protein interaction modules that predominate in submembranous scaffolding proteins. Recently, we showed that the PDZ domains of syntenin-1 also interact with phosphatidylinositol 4,5-bisphosphate (PIP2) and that this interaction controls the recruitment of the protein to the plasma membrane. Here we evaluate the general importance of PIP2-PDZ domain interactions. We report that most PDZ proteins bind weakly to PIP2, but that syntenin-2, the closest homolog of syntenin-1, binds with high affinity to PIP2 via its PDZ domains. Surprisingly, these domains target syntenin-2 to nuclear PIP2 pools, in nuclear speckles and nucleoli. Targeting to these sites is abolished by treatments known to affect these PIP2 pools. Mutational and domain-swapping experiments indicate that high-affinity binding to PIP2 requires both PDZ domains of syntenin-2, but that its first PDZ domain contains the nuclear PIP2 targeting determinants. Depletion of syntenin-2 disrupts the nuclear speckles-PIP2 pattern and affects cell survival and cell division. These findings show that PIP2-PDZ domain interactions can directly contribute to subnuclear assembly processes.
ISSN: 0261-4189
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Molecular Genetics Section (-)
Intellectual Property
Department of Human Genetics - miscellaneous
Laboratory for Cytogenetics and Genome Research
× corresponding author
# (joint) last author

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