High impact information on KAP114

• We demonstrate that Nap1p can bind directly to Kap114p, the primary karyopherin/importin responsible for the nuclear import of H2A and H2B [1].
• Importantly, we show that Kap114p, Kap121p, and Kap95 interact directly with both histone NLSs and that RanGTP inhibits this association [2].
• Deletion of the KAP114 gene led to specific mislocalization of TBP to the cytoplasm [3].
• Nuclear import of the TATA-binding protein: mediation by the karyopherin Kap114p and a possible mechanism for intranuclear targeting [3].
• Consistent with its role as a Sua7p import factor, deletion of KAP114 led to specific mislocalization of Sua7p to the cytoplasm [4].

Biological context of KAP114

• The importin/karyopherin Kap114 mediates the nuclear import of TATA-binding protein [5].

Anatomical context of KAP114

• A complex of Kap114p and TBP was detected in the cytosol and could be reconstituted using recombinant proteins, suggesting that the interaction was direct [3].

Physical interactions of KAP114

• Kap114 binds TBP in vitro, and binding is disrupted in the presence of GTPgammaS [5].

Regulatory relationships of KAP114

• Furthermore, we demonstrate that Nap1p promotes the association of the H2A and H2B NLSs specifically with the karyopherin Kap114p [1].

Other interactions of KAP114

• We conclude from our in vivo and in vitro experiments that import of the essential histones is mediated mainly by the essential importin Pse1p, while the non-essential Kap114p functions in a parallel import pathway for H2A and H2B [6].
• Nap1p also serves as a bridge between Kap114p and the histone nuclear localization sequence (NLS) [1].

References