Matches in UGent Biblio for { <https://biblio.ugent.be/publication/831804#aggregation> ?p ?o. }
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- aggregation classification "A1".
- aggregation creator B193030.
- aggregation creator B193031.
- aggregation creator B193032.
- aggregation creator B193033.
- aggregation creator B193034.
- aggregation creator B193035.
- aggregation creator B193036.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2009".
- aggregation format "application/pdf".
- aggregation hasFormat 831804.bibtex.
- aggregation hasFormat 831804.csv.
- aggregation hasFormat 831804.dc.
- aggregation hasFormat 831804.didl.
- aggregation hasFormat 831804.doc.
- aggregation hasFormat 831804.json.
- aggregation hasFormat 831804.mets.
- aggregation hasFormat 831804.mods.
- aggregation hasFormat 831804.rdf.
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- aggregation hasFormat 831804.txt.
- aggregation hasFormat 831804.xls.
- aggregation hasFormat 831804.yaml.
- aggregation isPartOf urn:issn:1420-682X.
- aggregation language "eng".
- aggregation publisher "BIRKHAUSER VERLAG AG".
- aggregation subject "Technology and Engineering".
- aggregation title "The PDZ2 domain of zonula occludens-1 and-2 is a phosphoinositide binding domain".
- aggregation 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.".
- aggregation authorList BK453938.
- aggregation endPage "3966".
- aggregation issue "24".
- aggregation startPage "3951".
- aggregation volume "66".
- aggregation aggregates 3112699.
- aggregation isDescribedBy 831804.
- aggregation similarTo s00018-009-0156-6.
- aggregation similarTo LU-831804.