Karyopherin alpha7 (KPNA7), a divergent member of the importin alpha family of nuclear import receptors.

BACKGROUND:Classical nuclear localization signal (NLS) dependent nuclear import is carried out by a heterodimer of importin alpha and importin beta. NLS cargo is recognized by importin alpha, which is bound by importin beta. Importin beta mediates translocation of the complex through the central channel of the nuclear pore, and upon reaching the nucleus, RanGTP binding to importin beta triggers disassembly of the complex. To date, six importin alpha family members, encoded by separate genes, have been described in humans. RESULTS:We sequenced and characterized a seventh member of the importin alpha family of transport factors, karyopherin alpha 7 which is most closely related to The domain of that binds Importin beta (IBB) is divergent, and shows stronger binding to importin beta than the IBB domains from of other importin alpha family members. With regard to NLS recognition, Kduanyu15357 binds to the retinoblastoma (RB) NLS to a similar degree as but it fails to bind the SV40-NLS and the human nucleoplasmin (NPM) NLS. Kduanyu15357 shows a predominantly nuclear distribution under steady state conditions, which contrasts with which is primarily is a novel importin alpha family member in humans that belongs to the importin alpha2 subfamily. Kduanyu15357 shows different subcellular localization and NLS binding characteristics compared to other members of the importin alpha family. These properties suggest that Kduanyu15357 could be specialized for interactions with select NLS-containing proteins, potentially impacting developmental regulation.

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