Access Restriction

Author Meerschaert, Kris ♦ Tun, Moe Phyu ♦ Remue, Eline ♦ Ganck, Ariane ♦ Boucherie, Ciska ♦ Vanloo, Berlinda ♦ Degeest, Gisèle ♦ Vandekerckhove, Joël ♦ Zimmermann, Pascale ♦ Bhardwaj, Nitin ♦ Lu, Hui ♦ Cho, Wonhwa ♦ Gettemans, Jan
Source SpringerLink
Content type Text
Publisher SP Birkhäuser Verlag Basel
File Format PDF
Copyright Year ©2009
Language English
Subject Domain (in DDC) Natural sciences & mathematics ♦ Life sciences; biology
Subject Keyword Tight junction ♦ Phospholipid ♦ Post synaptic density-discs large-zonula occludens ♦ Nucleus ♦ Cell polarity ♦ Biochemistry ♦ Life Sciences ♦ Biomedicine general ♦ Cell Biology
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 1420682X
Age Range 18 to 22 years ♦ above 22 year
Educational Use Research
Education Level UG and PG
Learning Resource Type Article
Publisher Date 2009-09-22
Publisher Place Basel
e-ISSN 14209071
Journal Cellular and Molecular Life Sciences
Volume Number 66
Issue Number 24
Page Count 16
Starting Page 3951
Ending Page 3966

Open content in new tab

   Open content in new tab
Source: SpringerLink