Title: Structural Diversity of PDZ-Lipid Interactions
Authors: Gallardo, Rodrigo
Ivarsson, Ylva
Schymkowitz, Joost
Rousseau, Frederic
Zimmermann, Pascale # ×
Issue Date: Mar-2010
Publisher: Wiley-v c h verlag gmbh
Series Title: Chembiochem vol:11 issue:4 pages:456-467
Abstract: PDZ domains are globular protein modules that are over-and-above appreciated for their interaction with short peptide motifs found in the cytosolic tail of membrane receptors, channels, and adhesion molecules. These domains predominate in scaffold molecules that control the assembly and the location of large signaling complexes. Studies have now emerged showing that PDZ domains can also interact with membrane lipids, and in particular with phosphoinositides. Phosphoinositides control various aspects of cell signaling, vesicular trafficking, and cytoskeleton remodeling. When investigated, lipid binding appears to be extremely relevant for PDZ protein functionality. Studies point to more than one mechanism for PDZ domains to associate with lipids. Few studies have been focused on the structural basis of PDZ-phosphoinositide interactions, and the biological consequences of such interactions. Using the current knowledge on syntenin-1, syntenin-2, PTP-Bas, PAR-3 and PICK1, we recapitulate our understanding of the structural and biochemical aspects of PDZ-lipid interactions and the consequences for peptide interactions.
ISSN: 1439-4227
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Laboratory for Signal Integration in Cell Fate Decision
Switch Laboratory
Department of Human Genetics - miscellaneous
× corresponding author
# (joint) last author

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