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Papers In Press, published online ahead of print January 4, 2005
Department of Molecular Biology and Biochemistry, Osaka University Graduate School of Medicine/Faculty of Medicine, Osaka 565-0871
Corresponding Author: ytakai{at}molbio.med.osaka-u.ac.jp
The Drosophila tumor suppressor protein lethal (2) giant larvae [l(2)gl] is involved in asymmetric cell division during development and epithelial cell polarity through interaction with the aPKC/Par-6 complex. We showed here that Lgl2, a mammalian homolog of l(2)gl, directly bound to LGN, a mammalian homolog of Partner of inscuteable in HEK293 cells. The C-terminal tail of Lgl2 bound to LGN with a Kd value of about 56 nM. Endogenous Lgl2 formed a complex with aPKC, Par-6, and LGN. This complex formation was enhanced in metaphase of the synchronized cells by treatment with thymidine and nocodazole. Immunofluorescence staining of the complex was the strongest at the cell periphery of the metaphase cells. Overexpression of the C-terminal tail of Lgl2 induced mis-localization of the nuclear mitotic apparatus protein NuMA and disorganization of the mitotic spindle during mitosis, eventually causing formation of multiple micronuclei. Knockdown of endogenous Lgl also induced disorganization of the mitotic spindle, thereby causing formation of multiple micronuclei. The binding between Lgl and LGN played a role in the mitotic spindle organization through regulating formation of the LGN-NuMA complex. These results indicate that Lgl2 forms a Lgl2/aPKC/Par-6/LGN complex which responds to mitotic signaling to establish normal cell division.
J. Biol. Chem, 10.1074/jbc.C400440200
Submitted on September 20, 2004
Revised on January 4, 2005
Accepted on January 2, 2005
Direct binding of Lgl2 to LGN during mitosis and its requirement for normal cell division
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