2003
DOI: 10.1038/ncb923
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Direct interaction of two polarity complexes implicated in epithelial tight junction assembly

Abstract: Tight junctions help establish polarity in mammalian epithelia by forming a physical barrier that separates apical and basolateral membranes. Two evolutionarily conserved multi-protein complexes, Crumbs (Crb)-PALS1 (Stardust)-PATJ (DiscsLost) and Cdc42-Par6-Par3-atypical protein kinase C (aPKC), have been implicated in the assembly of tight junctions and in polarization of Drosophila melanogaster epithelia. Here we identify a biochemical and functional link between these two complexes that is mediated by Par6 … Show more

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Cited by 455 publications
(406 citation statements)
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“…Distributions of other apical proteins, including aPKC and INADL (ref. 17; Fig. 5g-j), were also abnormal in neuroepithelium of hyh mutants.…”
Section: Nature Genetics Volume 36 | Number 3 | March 2004 267mentioning
confidence: 92%
“…Distributions of other apical proteins, including aPKC and INADL (ref. 17; Fig. 5g-j), were also abnormal in neuroepithelium of hyh mutants.…”
Section: Nature Genetics Volume 36 | Number 3 | March 2004 267mentioning
confidence: 92%
“…In COS7 cells, activated forms of Cdc42 can modulate the binding of Par-6 to Pals1, suggesting that there may be some functional connection between the CRIB motif and the PDZ domain of Par-6 (Hurd et al, 2003). Although Cdc42 binding does not seem to affect Par-6 binding to Pals1 in vitro, it does induce a~13-fold increase in binding affinity for the C terminus of an artificial peptide (-VKESLV-COOH).…”
Section: Provision Of Binding Sites For Multi-protein Assemblymentioning
confidence: 99%
“…The PDZ domain of Par-6 is one of the few known PDZ domains that has a binding groove capable of interacting with an internal protein segment (e.g., an N-terminal region of Pals1, a scaffold protein associated with tight junctions); but, it is also known to bind more classically to C-terminal motifs (e.g., the C terminus of Crb3, a small transmembrane protein) (Hurd et al, 2003;Lemmers et al, 2004;Penkert et al, 2004). In COS7 cells, activated forms of Cdc42 can modulate the binding of Par-6 to Pals1, suggesting that there may be some functional connection between the CRIB motif and the PDZ domain of Par-6 (Hurd et al, 2003).…”
Section: Provision Of Binding Sites For Multi-protein Assemblymentioning
confidence: 99%
“…The Par complex consists of the three homologues of Par6 (Par6a, Par6b, and Par6d), Par3 (Pard3 and Pard3b), the two atypical protein kinase C (aPKC) homologues, aPKCk and aPKCf, and Cdc42. The Crumbs complex and Par complex interact with each other by binding Par6 to either Crumbs [7] or Pals1 [8] (schematic summary shown in Fig. 2A).…”
Section: Introductionmentioning
confidence: 99%