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• W2097968191 abstract "The evolutionarily conserved Par-3/Par-6/aPKC complex is essential for the establishment and maintenance of polarity of a wide range of cells. Both Par-3 and Par-6 are PDZ domain containing scaffold proteins capable of binding to polarity regulatory proteins. In addition to three PDZ domains, Par-3 also contains a conserved N-terminal oligomerization domain (NTD) that is essential for proper subapical membrane localization and consequently the functions of Par-3. The molecular basis of NTD-mediated Par-3 membrane localization is poorly understood. Here, we describe the structure of a monomeric form of the Par-3 NTD. Unexpectedly, the domain adopts a PB1-like fold with both type-I and type-II structural features. The Par-3 NTD oligomerizes into helical filaments via front-to-back interactions. We further demonstrate that the NTD-mediated membrane localization of Par-3 in MDCK cells is solely attributed to its oligomerization capacity. The data presented in this study suggest that the Par-3 NTD is likely to facilitate the assembly of higher-order Par-3/Par-6/aPKC complex with increased avidities in targeting the complex to the subapical membrane domain and in binding to other polarity-regulating proteins." @default.
• W2097968191 created "2016-06-24" @default.
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• W2097968191 date "2007-05-03" @default.
• W2097968191 modified "2023-10-01" @default.
• W2097968191 title "The Par-3 NTD adopts a PB1-like structure required for Par-3 oligomerization and membrane localization" @default.
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• W2097968191 doi "https://doi.org/10.1038/sj.emboj.7601702" @default.
• W2097968191 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1888665" @default.
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