Article #6 Summary

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University of Toronto St. George
Cell and Systems Biology

CSB428H1F Article #6: Krahn et al. Formation of Baz-Sdt for epithelial polarity Introduction Baz phosphorylation site bind PDZ of Sdt to recruit Sdt to PM. Phosphorylation of Baz causes it to dissociate from Sdt. Non-phosphorylatable Baz blocks dissociation causing mutation similar to crb and sdt. Crb cytoplasmic domain binds PDZ domain of Sdt and Sdt recruit Patj and Lin-7 to apical complex. Dlg/Lgl/Scrib localize to lateral PM and antagonize Crb-Sdt complex, restricting apical expansion. BazS980 phosphorylation is required for localization S980E WT Baz-GFP and Baz -GFP shows the same localization basal to Crb-Sdt. Phosphorylated BazS980-P was concentrated in most apical part, sometimes with/without Crb-Sdt. WT Baz-GFP and Baz S98-GFP but not Baz S980-GFP rescued maternal and zygotic baz lethality. Overexpression of Baz S980-GFP is similar to crb and sdt Overexpression of Baz S980-GFP caused formation of aggregate containing DE-Cad, Arm, -cat, Par-6, aPKC, Crb, Sdt, Patj and Lin7. Lateral marker Dlg was normal. S980A Baz -GFP overexpression caused cells to round up and die of apoptosis. S980A These dominant-negative effects of Baz -GFP were sell-autonomous. Deletion of Baz CR1 or PDZ domains did not affect is dominancy. However, those lacking PM targeting signal was not dominant, showing Baz S980-GFP must be at PM to be dominant. S980A In neuroblasts and oocytes, Baz -GFP localize apically like WT and cell fate determinants, spindle orientation, cell division, and viability was not affected. S980A Baz -GFP mimic crb sdt crb sdt baz aPKC , and Par-6 mutants secrete only little scraps of cuticle. Overexpressing Baz S980-GFP caused a cuticle phenotype similar to crb or sdt mutants, but phe
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