High impact information on Patj

• Here, we describe a novel Drosophila protein, Discs Lost (DLT), that plays a crucial role in the polarization of embryonic epithelia during cellular blastoderm formation [1].
• A core component of the SAC is the transmembrane protein Crumbs, the cytoplasmic domain of which recruits the PDZ-protein Discs Lost into the complex [2].
• In Drosophila, this complex colocalizes with the Crumbs-Stardust (Sdt)-Pals1-associated TJ protein (Patj) complex [3].
• Discs Lost (Dlt), a cytoplasmic PDZ domain protein that was shown to interact with the cytoplasmic tail of Crb, overlaps precisely in its distribution with Crb, as shown by immunoelectron microscopy [4].
• We further demonstrate that Dlt directly binds to Par-6, providing a molecular basis for the mutual dependence of the two complexes [5].

Biological context of Patj

• DPATJ plays a role in retinal morphogenesis and protects against light-dependent degeneration of photoreceptor cells in the Drosophila eye [6].
• Our genetic analysis of hypomorph, null, and RNA interference reveals distinct dual functions of Dpatj in developing and mature photoreceptors [7].

Anatomical context of Patj

• We propose to rename this PDZ protein after its vertebrate homolog, Patj (Pals-associated tight junction protein) [8].
• Taken together, the data indicate that hINADl is likely to represent a Dlt homolog in mammalian epithelial cells and might be involved in regulating the integrity of tight junctions [9].
• Domain-specific early and late function of Dpatj in Drosophila photoreceptor cells [7].

References