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The Par-3 NTD adopts a PB1-like structure required for Par-3 oligomerization and membrane localization.

The Par-3 NTD adopts a PB1-like structure required for Par-3 oligomerization and membrane localization. Research Abstract Details 

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  • The Par-3 NTD adopts a PB1-like structure required for Par-3 oligomerization and membrane localization. Abstract Text:

    wei fengWei Feng,hao wuHao Wu,ling-nga chanLing-Nga Chan,mingjie zhangMingjie Zhang,

    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.

    The Par-3 NTD adopts a PB1-like structure required for Par-3 oligomerization and membrane localization. Publishing Authors By Initials

    w fengW Feng,h wuH Wu,ln chanLN Chan,m zhangM Zhang,

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    The Par-3 NTD adopts a PB1-like structure required for Par-3 oligomerization and membrane localization. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: The EMBO journal

    VOLUME: 26

    Page Numbers: 2786-96

    Journal Abbreviation: EMBO J.

    ISSN: 0261-4189

    DAY: 3

    MONTH: 05

    YEAR: 2007

    The Par-3 NTD adopts a PB1-like structure required for Par-3 oligomerization and membrane localization. Information

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    LANGUAGE: eng

    NlmUniqueID: 8208664

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    Grant and Affiliation Information for The Par-3 NTD adopts a PB1-like structure required for Par-3 oligomerization and membrane localization.

    AFFILIATION: Department of Biochemistry, Molecular Neuroscience Center, The Hong Kong University of Science and Technology, Kowloon, Hong Kong.

    Country: England

    England Research PublicationEngland Research Publication

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    MEDLINETA: EMBO J

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