In human importin [alpha], for example, there exists an [alpha]1 subfamily (importin [alpha]5 (KPNA1), [alpha]6 (KPNA5), and [alpha]7 (KPNA6)), [alpha]2 subfamily (importin [alpha]1 (KPNA2) and [alpha]8 (KPNA7)), and [alpha]3 subfamily (importin [alpha]3 (KPNA4) and [alpha]4 (KPNA3)) (Fig.
For example, the expression patterns of importin [alpha] subtypes were shown to change during cell differentiation processes, and, more importantly, its modulation clearly affects cell differentiation processes such as the differentiation of embryonic stem cells into neural cells (KPNA1 (73)), myoblasts into myotubes (KPNA2 (77)), or maturation of oligodendrocyte progenitors (KPNA1, (80) KPNA4 (78)).
(94) It has also been shown that, in undifferentiated ES cells, high expression of KPNA2 inhibited the nuclear translocation of the POU-domain transcription factors Brn2 or Oct6 through the binding of its atypical C-terminal region to these cargoes.
Karyopherin alpha 2 (KPNA2
) is associated with the natural resistance to Schistosoma japanicum infection in Microtus fortis.
Li et al., "Identification of miR-26 as a key mediator of estrogen stimulated cell proliferation by targeting CHD1, GREB1 and KPNA2
," Breast Cancer Research, vol.
Among them we discuss KPNA2 and PSMD12 genes, also deleted in the patients of Stewart, Bartnik, Vergult (patients 3 and 4), and Kury (patients 5 and 6) studies [5-8].
The deletion encompassed KPNA2 and PSMD12 which could be involved in the fetal phenotype associated with 17q24.1q24.2 deletion.
Shi et al., "Downregulation of KPNA2
in non-small-cell lung cancer is associated with Oct4 expression," Journal of Translational Medicine, vol.
In Figure 3, our results reveal that ADRM1 regulates KPNA2, which promotes proliferation, and is mediated by the aging-related proteins, HSP90B1, CALR, HSPA5, PDIA3, RPN1, and ECT2, the smoking-related proteins, HUWE1, HSPA5, and ECT2, and the epigenetic regulation of ENO1, HSP90B1, CALR, and PDIA3, through the SUP and ER signaling pathways.
miR1-2 and miR200b Mediate the Reduction of Cell Proliferation and Metastasis through KPNA2 and ECT2, Respectively.
It probably interacts with karyopherin alpha/KPNA1 and KPNA2
thereby increasing their affinity for basic-type nuclear localization signal harboring proteins such as viral matrix protein, thus facilitating the translocation of the viral proteins into the nucleus.
Gene-encoding proteins implied that nucleo-cytoplasmic transport was also overexpressed (KPNA2
, KPNB1, RANBP1, and RCC1).