Extensions of PSD-95/discs large/ZO-1 (PDZ) domains influence lipid binding and membrane targeting of syntenin-1.
Syntenin-1 is a PDZ protein involved in receptor recycling and clustering. Its two PDZ domains interact with various receptors and phosphoinositides, and are flanked by N- and C-terminal regions. Here, we report the identification of an autoinhibitory peptide stretch in the N-terminus that might be regulated by phosphorylation. We further establish that basic residues in the C-terminal region mediate electrostatic interactions with reconstituted liposomes and contribute to the plasma membrane targeting. Our study adds new components to the multi-dentate membrane targeting mechanism and highlights the role of N- and C-terminal PDZ extensions in the regulation of syntenin-1 plasma membrane localization.
Laboratory for Signal Integration in Cell Fate Decision, Department of Human Genetics, KU Leuven, Belgium.
Anna Maria
AM
Wawrzyniak
Elke
E
Vermeiren
Pascale
P
Zimmermann
Ylva
Y
Ivarsson
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D045744:Cell Line, Tumor; D002462:Cell Membrane / Q000378:metabolism; D000076122:Disks Large Homolog 4 Protein; D051528:Guanylate Kinases / Q000378:metabolism*; D006801:Humans; D050356:Lipid Metabolism; D008565:Membrane Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D054731:PDZ Domains; D010750:Phosphoproteins / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D055672:Static Electricity; D020349:Surface Plasmon Resonance; D053676:Syntenins / Q000737:chemistry / Q000378:metabolism*; D062826:Zonula Occludens-1 Protein
D000076122:Disks Large Homolog 4 Protein; C501447:Dlg4 protein, mouse; D008565:Membrane Proteins; D010750:Phosphoproteins; D053676:Syntenins; C569042:TJP1 protein, human; C569043:Tjp1 protein, mouse; D062826:Zonula Occludens-1 Protein; D051528:Guanylate Kinases