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• W1882963992 abstract "In vertebrates, the nuclear pore complex (NPC), the gate for transport of macromolecules between the nucleus and the cytoplasm, consists of approximately 30 different nucleoporins (Nups). The Nup and SUMO E3-ligase Nup358/RanBP2 are the major components of the cytoplasmic filaments of the NPC. In this study, we perform a structure-function analysis of Nup358 and describe its role in nuclear import of specific proteins. In a screen for nuclear proteins that accumulate in the cytoplasm upon Nup358 depletion, we identified proteins that were able to interact with Nup358 in a receptor-independent manner. These included the importin α/β-cargo DBC-1 (deleted in breast cancer 1) and DMAP-1 (DNA methyltransferase 1 associated protein 1). Strikingly, a short N-terminal fragment of Nup358 was sufficient to promote import of DBC-1, whereas DMAP-1 required a larger portion of Nup358 for stimulated import. Neither the interaction of RanGAP with Nup358 nor its SUMO-E3 ligase activity was required for nuclear import of all tested cargos. Together, Nup358 functions as a cargo- and receptor-specific assembly platform, increasing the efficiency of nuclear import of proteins through various mechanisms." @default.
• W1882963992 created "2016-06-24" @default.
• W1882963992 creator A5001395737 @default.
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• W1882963992 creator A5081435154 @default.
• W1882963992 date "2011-11-21" @default.
• W1882963992 modified "2023-10-14" @default.
• W1882963992 title "The Nucleoporin Nup358/RanBP2 Promotes Nuclear Import in a Cargo- and Transport Receptor-Specific Manner" @default.
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• W1882963992 doi "https://doi.org/10.1111/j.1600-0854.2011.01302.x" @default.
• W1882963992 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21995724" @default.
• W1882963992 hasPublicationYear "2011" @default.
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