The Ser/Thr kinases of the PAR-1/MARK/Kin1 family are conserved regulators of polarity in epithelial and non-epithelial cells [1]. Drosophila PAR-1 localizes laterally in the follicular epithelium of the ovary [2, 3], where it has been shown to function at two distinct levels: It stabilizes the cytoskeleton [3, 4] and it regulates apical-basal polarity by directly inhibiting lateral assembly of the apical aPKC/Bazooka/PAR-6 complex [5, 6]. However, it has been unclear how lateral localization of Drosophila PAR-1 is achieved and whether this localization contributes to epithelial polarity in vivo. Here we show that, through its spacer domain, Drosophila PAR-1 accumulates on the lateral plasma membrane (PM) in cells of the follicular epithelium (FE). Rescue experiments indicate that in FE cells PAR-1 kinase activity is essential for all the described functions of PAR-1. In contrast, the spacer domain of PAR-1 is required for apical-basal polarity and growth control but is dispensable for microtubule (MT) stabilization. Our data indicate that the spacer domain of PAR-1 is required for lateral PM localization of PAR-1 kinase and for development of a polarized FE.

The Drosophila PAR-1 spacer domain is required for lateral membrane association and for polarization of follicular epithelial cells / T. Vaccari, C. Rabouille, A. Ephrussi. - In: CURRENT BIOLOGY. - ISSN 0960-9822. - 15:3(2005), pp. 255-261.

The Drosophila PAR-1 spacer domain is required for lateral membrane association and for polarization of follicular epithelial cells

T. Vaccari
Primo
;
2005

Abstract

The Ser/Thr kinases of the PAR-1/MARK/Kin1 family are conserved regulators of polarity in epithelial and non-epithelial cells [1]. Drosophila PAR-1 localizes laterally in the follicular epithelium of the ovary [2, 3], where it has been shown to function at two distinct levels: It stabilizes the cytoskeleton [3, 4] and it regulates apical-basal polarity by directly inhibiting lateral assembly of the apical aPKC/Bazooka/PAR-6 complex [5, 6]. However, it has been unclear how lateral localization of Drosophila PAR-1 is achieved and whether this localization contributes to epithelial polarity in vivo. Here we show that, through its spacer domain, Drosophila PAR-1 accumulates on the lateral plasma membrane (PM) in cells of the follicular epithelium (FE). Rescue experiments indicate that in FE cells PAR-1 kinase activity is essential for all the described functions of PAR-1. In contrast, the spacer domain of PAR-1 is required for apical-basal polarity and growth control but is dispensable for microtubule (MT) stabilization. Our data indicate that the spacer domain of PAR-1 is required for lateral PM localization of PAR-1 kinase and for development of a polarized FE.
Amino Acid Sequence; Animals; Blotting, Western; Cell Membrane; Cell Polarity; Cells, Cultured; DNA Primers; Drosophila Proteins; Drosophila melanogaster; Epithelium; Female; Fluorescent Antibody Technique; Glycogen Synthase Kinase 3; Green Fluorescent Proteins; Microscopy, Electron, Transmission; Molecular Sequence Data; Ovarian Follicle; Protein Kinases; Protein Structure, Tertiary; Protein-Serine-Threonine Kinases; Sequence Alignment; Sequence Analysis, DNA; Transgenes; Agricultural and Biological Sciences (all)
Settore BIO/13 - Biologia Applicata
2005
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/493189
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