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

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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.
Keywords
DIMERIZATION, DISEASE, SIGNAL, PLECKSTRIN HOMOLOGY DOMAINS, JUNCTION PROTEIN ZO-2, EPITHELIAL-CELLS, PLASMA-MEMBRANE, TIGHT JUNCTIONS, LOCALIZATION, NUCLEUS

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Citation

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Chicago
Meerschaert, Kris, Moe Phyu Tun, Eline Remue, Ariane De Ganck, Ciska Boucherie, Berlinda Vanloo, Gisele Degeest, et al. 2009. “The PDZ2 Domain of Zonula Occludens-1 and-2 Is a Phosphoinositide Binding Domain.” Cellular and Molecular Life Sciences 66 (24): 3951–3966.
APA
Meerschaert, K., Tun, M. P., Remue, E., De Ganck, A., Boucherie, C., Vanloo, B., Degeest, G., et al. (2009). The PDZ2 domain of zonula occludens-1 and-2 is a phosphoinositide binding domain. CELLULAR AND MOLECULAR LIFE SCIENCES, 66(24), 3951–3966.
Vancouver
1.
Meerschaert K, Tun MP, Remue E, De Ganck A, Boucherie C, Vanloo B, et al. The PDZ2 domain of zonula occludens-1 and-2 is a phosphoinositide binding domain. CELLULAR AND MOLECULAR LIFE SCIENCES. BASEL: BIRKHAUSER VERLAG AG; 2009;66(24):3951–66.
MLA
Meerschaert, Kris et al. “The PDZ2 Domain of Zonula Occludens-1 and-2 Is a Phosphoinositide Binding Domain.” CELLULAR AND MOLECULAR LIFE SCIENCES 66.24 (2009): 3951–3966. Print.
@article{831804,
  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.},
  author       = {Meerschaert, Kris and Tun, Moe Phyu and Remue, Eline and De Ganck, Ariane and Boucherie, Ciska and Vanloo, Berlinda and Degeest, Gisele and Vandekerckhove, Jo{\"e}l and Zimmermann, Pascale and Bhardwaj, Nitin and Lu, Hui and Cho, Wonhwa and Gettemans, Jan},
  issn         = {1420-682X},
  journal      = {CELLULAR AND MOLECULAR LIFE SCIENCES},
  language     = {eng},
  number       = {24},
  pages        = {3951--3966},
  publisher    = {BIRKHAUSER VERLAG AG},
  title        = {The PDZ2 domain of zonula occludens-1 and-2 is a phosphoinositide binding domain},
  url          = {http://dx.doi.org/10.1007/s00018-009-0156-6},
  volume       = {66},
  year         = {2009},
}

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