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- W2132856536 abstract "SUMOylation is a form of post-translational modification shown to control nuclear transport. Krüppel-like factor 5 (KLF5) is an important mediator of cell proliferation and is primarily localized to the nucleus. Here we show that mouse KLF5 is SUMOylated at lysine residues 151 and 202. Mutation of these two lysines or two conserved nearby glutamates results in the loss of SUMOylation and increased cytoplasmic distribution of KLF5, suggesting that SUMOylation enhances nuclear localization of KLF5. Lysine 151 is adjacent to a nuclear export signal (NES) that resembles a consensus NES. The NES in KLF5 directs a fused green fluorescence protein to the cytoplasm, binds the nuclear export receptor CRM1, and is inhibited by leptomycin and site-directed mutagenesis. SUMOylation facilitates nuclear localization of KLF5 by inhibiting this NES activity, and enhances the ability of KLF5 to stimulate anchorage-independent growth of HCT116 colon cancer cells. A survey of proteins whose nuclear localization is regulated by SUMOylation reveals that SUMOylation sites are frequently located in close proximity to NESs. A relatively common mechanism for SUMOylation to regulate nucleocytoplasmic transport may lie in the interplay between neighboring NES and SUMOylation motifs." @default.
- W2132856536 created "2016-06-24" @default.
- W2132856536 creator A5000994247 @default.
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- W2132856536 creator A5023914766 @default.
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- W2132856536 date "2008-11-01" @default.
- W2132856536 modified "2023-10-14" @default.
- W2132856536 title "SUMOylation Regulates Nuclear Localization of Krüppel-like Factor 5" @default.
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- W2132856536 doi "https://doi.org/10.1074/jbc.m803612200" @default.
- W2132856536 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2581587" @default.
- W2132856536 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18782761" @default.
- W2132856536 hasPublicationYear "2008" @default.
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