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The PDZ2 domain of zonula occludens-1 and -2 is a phosphoinositide binding domain.


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.

SUBMITTER: Meerschaert K 

PROVIDER: S-EPMC3724457 | biostudies-literature | 2009 Dec

REPOSITORIES: biostudies-literature

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The PDZ2 domain of zonula occludens-1 and -2 is a phosphoinositide binding domain.

Meerschaert Kris K   Tun Moe Phyu MP   Remue Eline E   De Ganck Ariane A   Boucherie Ciska C   Vanloo Berlinda B   Degeest Gisèle G   Vandekerckhove Joël J   Zimmermann Pascale P   Bhardwaj Nitin N   Lu Hui H   Cho Wonhwa W   Gettemans Jan J  

Cellular and molecular life sciences : CMLS 20090922 24


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 no  ...[more]

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