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Title: The PDZ2 domain of zonula occludens-1 and -2 is a phosphoinositide binding domain
Authors: Meerschaert, Kris
Tun, Moe
Remue, Eline
De Ganck, Ariane
Boucherie, Ciska
Vanloo, Berlinda
Degeest, Gisèle
Vandekerckhove, Joël
Zimmermann, Pascale
Bhardwaj, Nitin
Lu, Hui Qi
Cho, Wonhwa
Gettemans, Jan # ×
Issue Date: Dec-2009
Publisher: Birkhäuser Verlag
Series Title: Cellular and Molecular Life Sciences vol:66 issue:24 pages:3951-3966
Abstract: Zonula occludens proteins (ZO) are postsynaptic density protein-95 discs large-zonula occludens (PDZ) domain-containing proteins that play a fundamental role in the assembly of tight junctions and establishment of cell polarity. Here, we show that the second PDZ domain of ZO-1 and ZO-2 binds phosphoinositides (PtdInsP) and we identified critical residues involved in the interaction. Furthermore, peptide and PtdInsP binding of ZO PDZ2 domains are mutually exclusive. Although lipid binding does not seem to be required for plasma membrane localisation of ZO-1, phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P (2)) binding to the PDZ2 domain of ZO-2 regulates ZO-2 recruitment to nuclear speckles. Knockdown of ZO-2 expression disrupts speckle morphology, indicating that ZO-2 might play an active role in formation and stabilisation of these subnuclear structures. This study shows for the first time that ZO isoforms bind PtdInsPs and offers an alternative regulatory mechanism for the formation and stabilisation of protein complexes in the nucleus.
ISSN: 1420-682X
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Department of Human Genetics - miscellaneous
× corresponding author
# (joint) last author

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