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Published online
doi:10.1083/jcb.200612022
The Journal of Cell Biology, Vol. 178, No. 4, 575-581
The Rockefeller University Press, 0021-9525 $30.00
© Bialucha et al.
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p32 is a novel mammalian Lgl binding protein that enhances the activity of protein kinase C{zeta} and regulates cell polarity



Carl U. Bialucha1, Emma C. Ferber1, Franck Pichaud1,2, Sew Y. Peak-Chew4, and Yasuyuki Fujita1,3

1 Medical Research Council Laboratory for Molecular Cell Biology and Cell Biology Unit, 2 Department of Anatomy and Developmental Biology, and 3 Department of Biology, University College London, London WC1E 6BT, England, UK
4 Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 2QH, England, UK

Correspondence to Yasuyuki Fujita: y.fujita{at}ucl.ac.uk

Lgl (lethal giant larvae) plays an important role in cell polarity. Atypical protein kinase C (aPKC) binds to and phosphorylates Lgl, and the phosphorylation negatively regulates Lgl activity. In this study, we identify p32 as a novel Lgl binding protein that directly binds to a domain on mammalian Lgl2 (mLgl2), which contains the aPKC phosphorylation site. p32 also binds to PKC{zeta}, and the three proteins form a transient ternary complex. When p32 is bound, PKC{zeta} is stimulated to phosphorylate mLgl2 more efficiently. p32 overexpression in Madin–Darby canine kidney cells cultured in a 3D matrix induces an expansion of the actin-enriched apical membrane domain and disrupts cell polarity. Addition of PKC{zeta} inhibitor blocks apical actin accumulation, which is rescued by p32 overexpression. p32 knockdown by short hairpin RNA also induces cell polarity defects. Collectively, our data indicate that p32 is a novel regulator of cell polarity that forms a complex with mLgl2 and aPKC and enhances aPKC activity.

Abbreviations used in this paper: aPKC, atypical PKC; HEK, human embryonic kidney; Lgl, lethal giant larvae; MBP, maltose binding protein; mLgl, mammalian Lgl; shRNA, short hairpin RNA; WT, wild type; ZO-1, zonula occludens-1.


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