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The Importin beta-dependent nuclear import of TopBP1 (show TOPBP1 Proteins) was required for the mitomycin C -induced Chk1 (show CHEK1 Proteins) phosphorylation.
Data show that importin-beta binds to Apc (show APC Proteins) and negatively regulates the MT-assembly and spindle-promoting activity of Apc (show APC Proteins) in a Ran-regulatable manner.
The initial step of chromatin seeding is negatively regulated by importin beta.
Study identified that high expression of Kpnbeta1 in breast cancer (BC) often leads to poor prognosis and that Kpnbeta1-knockdown markedly reduced BC cell proliferation by abrogating nuclear transport of Her2 (show ERBB2 Proteins).
Data suggest that IGFBP5 (show IGFBP5 Proteins) nuclear import is mediated by KPNA5 (show KPNA5 Proteins)/KPNB1 complex; nuclear localization sequence of IGFBP5 (show IGFBP5 Proteins) is critical domain in this nuclear translocation. (IGFBP5 (show IGFBP5 Proteins) = insulin-like growth factor binding protein-5 (show IGFBP5 Proteins); KPNA5 (show KPNA5 Proteins) = karyopherin subunit alpha-5 (show KPNA5 Proteins); KPNB1 = karyopherin subunit beta-1/importin-beta)
KPNB1 and Ran protein jointly mediated the nuclear import of NDV M protein (show MYOM2 Proteins), showing that KPNB1 protein interacted with NDV M protein (show MYOM2 Proteins) to form binary complex and then entered into the nucleus with the assistance of Ran protein.
Results show that importin beta1 is an Epac1 (show RAPGEF3 Proteins) binding partner that regulates Epac1 (show RAPGEF3 Proteins) subcellular localization.
Results found KPNB1 to be required for the migration and invasion of cervical cancer cells through mediating nuclear import. Its inhibition of KPNB1 interferes with NFkB subcellular localization.
These results showed that BLM enters the nucleus via the importin beta1, RanGDP and NTF2 dependent pathway, demonstrating for the first time the nuclear trafficking mechanism of a DNA helicase.
Karyoppherins constitute integral constituents of the nuclear pore complex whose barrier, transport, and cargo release functionalities establish a continuum under a mechanism of Kap (show CDKN3 Proteins)-centric control.
Therefore, we show for the first time that the nuclear localization of Cat L and its substrate Cux1can be positively regulated by Snail NLS and importin beta1, suggesting that Snail, Cat L and Cux1 all utilize importin beta1 for nuclear import.
KPNB1 might enhance human glioma proliferation via Wnt (show WNT2 Proteins)/beta-Catenin (show CTNNB1 Proteins) Pathway.
Importins, Impbeta, Kapbeta2, Imp4 (show SPPL2B Proteins), Imp5 (show IPO5 Proteins), Imp7 (show IPO7 Proteins), Imp9 (show IPO9 Proteins), and Impalpha, show the H3 tail binding more tightly than the H4 tail. The H3 tail binds Kapbeta2 and Imp5 (show IPO5 Proteins) with KD values of 77 and 57 nm, respectively, and binds the other five Importins more weakly.
KPNb1 acts as a positive regulator in the NF-kappaB (show NFKB1 Proteins) pathway to enhance palmitate-induced inflammation response.
KPNB1 may play a key role in the inflammation process of rheumatoid arthritis via STAT3 (show STAT3 Proteins) signal transduction pathway.
The study revealed a regulatory role of the p97 (show EIF4G2 Proteins)-Npl4-Ufd1 (show UFD1L Proteins) complex in regulating a partial degradation of the NF-kappaB (show NFKB1 Proteins) subunit p100 (show PATL2 Proteins).
Identification of a karyopherin beta1/beta2 proline-tyrosine nuclear localization signal in huntingtin (show HTT Proteins) protein.
translation of Importin beta1 mRNA enables separation of cytoplasmic and nuclear transport functions of importins and is required for efficient retrograde signaling in injured axons.
A critical function of RanBP2 is to capture recycling RanGTP-importin-beta complexes at cytoplasmic fibrils to allow for adequate classical nuclear localization signal-mediated cargo import.
Ap4A hydrolase (show NUDT2 Proteins) was found to translocate into the nuclei of mast cells following immunological activation; found its immunologically dependent association with importin beta
Data show that MRTF-A contains an unusually long bipartite nuclear localisation signal embedded within the RPEL domain, that uses the importin (Imp (show BRAP Proteins))alpha/beta-dependent import pathway, and that import is inhibited by G-actin (show ACTB Proteins).
results show the crystal structure of importin-beta complexed with the active form of SREBP-2 (show SREBF2 Proteins)
Results suggest that the importin alpha/beta system is involved in nuclear entry of mammalian clock components Cry2 (show CRY2 Proteins) and Per2 (show PER2 Proteins), which is indispensable to transcriptional oscillation of clock genes
Nucleocytoplasmic transport, a signal- and energy-dependent process, takes place through nuclear pore complexes embedded in the nuclear envelope. The import of proteins containing a nuclear localization signal (NLS) requires the NLS import receptor, a heterodimer of importin alpha and beta subunits also known as karyopherins. Importin alpha binds the NLS-containing cargo in the cytoplasm and importin beta docks the complex at the cytoplasmic side of the nuclear pore complex. In the presence of nucleoside triphosphates and the small GTP binding protein Ran, the complex moves into the nuclear pore complex and the importin subunits dissociate. Importin alpha enters the nucleoplasm with its passenger protein and importin beta remains at the pore. Interactions between importin beta and the FG repeats of nucleoporins are essential in translocation through the pore complex. The protein encoded by this gene is a member of the importin beta family. Two transcript variants encoding different isoforms have been found for this gene.
Importin beta-1 subunit
, importin beta-1 subunit
, importin beta 1
, importin 1
, importin 90
, importin subunit beta-1
, karyopherin subunit beta-1
, nuclear factor p97
, pore targeting complex 97 kDa subunit
, importin beta
, Importin beta
, karyopherin,beta 1
, nuclear factor P97