Chromatin-bound NLS proteins recruit membrane vesicles and nucleoporins for nuclear envelope assembly via importin-α/β

Quanlong Lu, Zhigang Lu, Qinying Liu, Li Guo, He Ren, Jingyan Fu, Qing Jiang, Paul R. Clarke, Chuanmao Zhang

    Research output: Contribution to journalArticle

    11 Citations (Scopus)

    Abstract

    The mechanism for nuclear envelope (NE) assembly is not fully understood. Importin-ß and the small GTPase Ran have been implicated in the spatial regulation of NE assembly process. Here we report that chromatin-bound NLS (nuclear localization sequence) proteins provide docking sites for the NE precursor membrane vesicles and nucleoporins via importin-a and -ß during NE assembly in Xenopus egg extracts. We show that along with the fast recruitment of the abundant NLS proteins such as nucleoplasmin and histones to the demembranated sperm chromatin in the extracts, importin-a binds the chromatin NLS proteins rapidly. Meanwhile, importin-ß binds cytoplasmic NE precursor membrane vesicles and nucleoporins. Through interacting with importin-a on the chromatin NLS proteins, importin-ß targets the membrane vesicles and nucleoporins to the chromatin surface. Once encountering Ran-GTP on the chromatin generated by RCC1, importin-ß preferentially binds Ran-GTP and releases the membrane vesicles and nucleoporins for NE assembly. NE assembly is disrupted by blocking the interaction between importin-a and NLS proteins with excess soluble NLS proteins or by depletion of importin-ß from the extract. Our findings reveal a novel molecular mechanism for NE assembly in Xenopus egg extracts.Cell Research advance online publication 31 July 2012; doi:10.1038/cr.2012.113.
    Original languageEnglish
    Pages (from-to)1562-1575
    Number of pages14
    JournalCell Research
    Volume22
    DOIs
    Publication statusPublished - Nov 2012

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