Anti-Importin-8

Importin-8 is a member of a class of approximately 20 potential Ran targets that share a sequence motif related to the Ran-binding site of importin-beta. It acts as a nuclear protein involved in the nucleolar transport. Importin-8 is required for cytoplasmic miRNA-guided gene silencing and is involved in loading Ago complexes into a variety of different mRNA targets, affecting the nuclear localization of Ago proteins. This protein binds to the nuclear pore complex and, along with RanGTP and RANBP1, inhibits the GAP stimulation of the Ran GTPase. The importin-alpha/beta complex and the GTPase Ran mediate nuclear import of proteins with a classical nuclear localization signal. Importin-8 has been proposed previously as a reference gene in the human motor cortex as it showed no differences in a study with different brain regions from chronic alcoholics and control subjects and lung samples. Protein function: Seems to function in nuclear protein import, either by acting as autonomous nuclear transport receptor or as an adapter- like protein in association with the importin-beta subunit KPNB1. Acting autonomously, is thought to serve itself as receptor for nuclear localization signals (NLS) and to promote translocation of import substrates through the nuclear pore complex (NPC) by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. In vitro mediates the nuclear import of SRP19. [The UniProt Consortium]