The Par complex directs asymmetric cell division by phosphorylating the cytoskeletal protein Lgl

Jörg Betschinger, Karl Mechtler and Juergen A. Knoblich ()
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Jörg Betschinger: Research Institute of Molecular Pathology
Karl Mechtler: Research Institute of Molecular Pathology
Juergen A. Knoblich: Research Institute of Molecular Pathology

Nature, 2003, vol. 422, issue 6929, 326-330

Abstract: Abstract To generate different cell types, some cells can segregate protein determinants into one of their two daughter cells during mitosis. In Drosophila neuroblasts, the Par protein complex localizes apically1,2,3,4,5 and directs localization of the cell fate determinants Prospero6,7,8 and Numb9 and the adaptor proteins Miranda10,11 and Pon12 to the basal cell cortex, to ensure their segregation into the basal daughter cell. The Par protein complex has a conserved function in establishing cell polarity13 but how it directs proteins to the opposite side is unknown. We show here that a principal function of this complex is to phosphorylate the cytoskeletal protein Lethal (2) giant larvae (Lgl; also known as L(2)gl). Phosphorylation by Drosophila atypical protein kinase C (aPKC), a member of the Par protein complex, releases Lgl from its association with membranes and the actin cytoskeleton. Genetic and biochemical experiments show that Lgl phosphorylation prevents the localization of cell fate determinants to the apical cell cortex. Lgl promotes cortical localization of Miranda14,15, and we propose that phosphorylation of Lgl by aPKC at the apical neuroblast cortex restricts Lgl activity and Miranda localization to the opposite, basal side of the cell.

Date: 2003
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DOI: 10.1038/nature01486

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