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lüll The unique-5 and -6 motifs of ZO-1 regulate tight junction strand localization and scaffolding properties Fanning AS; Little BP; Rahner C; Utepbergenov D; Walther Z; Anderson JMMol Biol Cell 2007[Mar]; 18 (3): 721-31The proper cellular location and sealing of tight junctions is assumed to depend on scaffolding properties of ZO-1, a member of the MAGUK protein family. ZO-1 contains a conserved SH3-GUK module that is separated by a variable region (unique-5), which in other MAGUKs has proven regulatory functions. To identify motifs in ZO-1 critical for its putative scaffolding functions, we focused on the SH3-GUK module including unique-5 (U5) and unique-6 (U6), a motif immediately C-terminal of the GUK domain. In vitro binding studies reveal U5 is sufficient for occludin binding; U6 reduces the affinity of this binding. In cultured cells, U5 is required for targeting ZO-1 to tight junctions and removal of U6 results in ectopically displaced junction strands containing the modified ZO-1, occludin, and claudin on the lateral cell membrane. These results provide evidence that ZO-1 can control the location of tight junction transmembrane proteins and reveals complex protein binding and targeting signals within its SH3-U5-GUK-U6 region. We review these findings in the context of regulated scaffolding functions of other MAGUK proteins.|Amino Acid Motifs[MESH]|Animals[MESH]|Binding Sites[MESH]|Dogs[MESH]|Freeze Fracturing[MESH]|Membrane Proteins/*chemistry/*metabolism[MESH]|Occludin[MESH]|Peptides/metabolism[MESH]|Phosphoproteins/*chemistry/*metabolism[MESH]|Protein Binding[MESH]|Protein Transport[MESH]|Tight Junctions/*metabolism[MESH]|Transgenes[MESH]|Zonula Occludens-1 Protein[MESH]|src Homology Domains[MESH] |