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Human KPNA2 Protein expressed in Wheat germ - ABIN1308916
Wang, Wang, Wang, Chen, Wu, Liang, Tsai, Chang, Yu, Yu: Importin subunit alpha-2 is identified as a potential biomarker for non-small cell lung cancer by integration of the cancer cell secretome and tissue transcriptome. in International journal of cancer. Journal international du cancer 2011
Nuclear import rates correlated with nuclear size, and varying the concentrations of two transport factors, importin alpha and Ntf2 (show NUTF2 Proteins), was sufficient to account for nuclear scaling between the two species.
a decreased H7N9 influenza A virus polymerase activity when importin-alpha7 was silenced by siRNA, is reported.
Results demonstrated that radiation-induced dying colorectal cancer cells released considerable amounts of KPNA2 that induce the maturation and activation of DCs for synergistic antitumor effect of radiation.
mTORC1 positively regulated the importer protein KPNA2, which participated in glycolysis regulation downstream of mTORC1 in a HIF1alpha (show HIF1A Proteins)-independent manner, indicating that mTORC1 regulates glycolysis through multiple ways.
provided support for a link between autophagy and epithelial-to-mesenchymal (-like) transition status in WT TP53 (show TP53 Proteins) glioblastoma cells and provided evidence for the signaling pathway (MIR517C-KPNA2-cytoplasmic TP53 (show TP53 Proteins)) involved in attenuating autophagy
Structure of importin-alpha bound to a non-classical nuclear localization signal of the influenza A virus nucleoprotein has been reported.
Specific interaction with the nuclear transporter (show RPAIN Proteins) importin alpha2 can modulate paraspeckle protein 1 (show PSPC1 Proteins) delivery to nuclear paraspeckles.
constitutive expression of Kpna2 during the differentiation culture of ESCs (show NR2E3 Proteins) significantly impairs clock development, and KPNA2 facilitates cytoplasmic localization of PER1 (show PER1 Proteins)/
a significant correlation of KPNA2 expression and tumour aggressiveness in a large variety of other solid tumour entities
study reports a cell-fate determination mechanism in which importin alpha2 negatively regulates the nuclear import of certain transcription factors to maintain embryonic stem cell properties
importin alpha binds to Nup153 (show NUP153 Proteins)
miR (show MLXIP Proteins)-26b plays an anti-metastatic role and is downregulated in gastric cancer tissues via the KPNA2/c-jun (show JUN Proteins) pathway
our results show for the first time that KPNA2 is transcriptionally and post-translationally regulated by the mTOR (show FRAP1 Proteins) pathway and provide new insights into targeted therapy for non-small cell lung cancer
KPNA2 was associated with tumorigenesis and cancer progression in CRC (show CALR Proteins) cells; high KPNA2 expression was associated with increased cell proliferation, migration, invasion, and semisolid agar colony formation.
that the interactions observed between TNRC6A and importin-alpha are conserved between mouse and human complexes. Our results highlight the ability of monopartite cNLS sequences to maximise contacts at the importin-alpha major binding site, as well as regions outside the main binding cavities.
The authors identified Importin-alpha1 to bind to Coxiella burnetii AnkG and concluded that binding of AnkG to p32 and Importin-alpha1 is essential for its migration into the nucleus.
the crystal structure of the nuclear import adaptor importin-alpha1 bound to the nuclear localization signal (NLS (show ALDH1A2 Proteins)) of EBNA-LP that shows EBNA-LP residues 44-RRVRRR-49 binding to the major NLS (show ALDH1A2 Proteins)-binding site at the P0-P5 positions.
High serum karyopherin alpha 2 levels (>485 microg/mL) correlated with International Federation of Gynecology and Obstetrics stage ( p < 0.0001), lymphatic metastasis ( p = 0.045), overall survival ( p = 0.001), and disease-free progression ( p = 0.006). Serum karyopherin alpha 2 represents a potential diagnostic biomarker for epithelial ovarian carcinoma.
p53 (show TP53 Proteins)/p21Cip1/Waf1 (show CDKN1A Proteins)/p16INK4a may be an important pathway involved in the function of KPNA2 in tongue squamous cell carcinoma (TSCC) CAL (show FBLIM1 Proteins)-27 cells.
These results suggest that the selected aptamers (76 and 72) warrant further study to explore not only their application in cancer diagnosis but also their use as a specific reagent to potentially block KPNA2-dependent nuclear transport of macromolecules across the nuclear membrane.
Authors demonstrated that swine importin alpha1 interacts with the M1 protein and transports it to the nucleus.
The import of proteins into the nucleus is a process that involves at least 2 steps. The first is an energy-independent docking of the protein to the nuclear envelope and the second is an energy-dependent translocation through the nuclear pore complex. Imported proteins require a nuclear localization sequence (NLS) which generally consists of a short region of basic amino acids or 2 such regions spaced about 10 amino acids apart. Proteins involved in the first step of nuclear import have been identified in different systems. These include the Xenopus protein importin and its yeast homolog, SRP1 (a suppressor of certain temperature-sensitive mutations of RNA polymerase I in Saccharomyces cerevisiae), which bind to the NLS. KPNA2 protein interacts with the NLSs of DNA helicase Q1 and SV40 T antigen and may be involved in the nuclear transport of proteins. KPNA2 also may play a role in V(D)J recombination
importin subunit alpha-2
, Importin subunit alpha-2
, karyopherin subunit alpha-2
, RAG cohort protein 1
, importin alpha P1
, importin subunit alpha-1
, pore targeting complex 58 kDa subunit
, karyopherin (importin) alpha 2
, nuclear import protein
, RAG cohort 1
, importin alpha 1
, importin alpha 2
, importin subunit alpha-8
, karyopherin subunit alpha-7
, nuclear transport receptor