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Experiments in Xenopus assembly extracts with M9M, a superaffinity nuclear localization sequence that displaces cargoes bound by transportin, or TLB, a mutant transportin that can bind cargo and RanGTP simultaneously, support direct inhibition.
Results indicate that TRN1 positively regulates miRNA activity by promoting the association of miRNAs with AGO1 (show EIF2C1 Proteins), and they reveal opposing roles of two importin beta (show KPNB1 Proteins) family proteins in miRNA loading.
Results show that tranportin 1 (AtTRN1) recognizes a broad spectrum of proteins having diverse functions, which will potentially be the cargoes of AtTRN1.
These results suggest that Aqp0a is the primary water channel (show AQP4 Proteins) of the lens and that Aqp0b, though possibly a secondary water channel (show AQP4 Proteins), has an unidentified function in the lens.
the TNPO1-Rab8 (show RAB8A Proteins)-ciliary targeting signals complex mediates selective entry into and retention of cargos within cilia.
SIN1 (show MAPKAP1 Proteins) plays an important role in non-small cell lung cancer; SIN1 (show MAPKAP1 Proteins) is a potential biomarker and a promising target in the treatment of NSCLC
This study provides evidence that Sin1 (show MAPKAP1 Proteins), a known element of the mammalian target of rapamycin (show FRAP1 Proteins) complex 2 (mTORC2 (show CRTC2 Proteins)), is required for Interferon-gamma (show IFNG Proteins)-induced phosphorylation and activation of AKT (show AKT1 Proteins) and that such activation mediates downstream regulation of mTORC1 and its effectors.
Together, these results indicate that transportin-1 mediates YB-1 (show YBX1 Proteins) nuclear translocation.
findings suggest that a new player, i.e., O-GlcNAcylation, regulates hnRNP A1 translocation and interaction with Trn1, possibly affecting its function
Intracellular localization of mTORC2 (show CRTC2 Proteins) component, mSin1, contributes to regulation of Akt (show AKT1 Proteins) phosphorylation.
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.
Results show that Karyopherin-b2 binds to the N-terminal tail of histone H3 (show HIST3H3 Proteins) with high affinity even though H3 lacks a recognizable proline-tyrosine nuclear localization signal (PY-NLS (show ALDH1A2 Proteins)).
FGF2 (show FGF2 Proteins) nuclear translocation is regulated by Karyopherin-beta2 and Ran GTPase (show RAN Proteins) in human glioblastoma cells
Akt (show AKT1 Proteins) phosphorylates SIN1 (show MAPKAP1 Proteins) at T86, enhancing mTORC2 (show CRTC2 Proteins) kinase activity, which leads to phosphorylation of Akt (show AKT1 Proteins) S473 by mTORC2 (show CRTC2 Proteins), thereby catalyzing full activation of Akt (show AKT1 Proteins).
Co-immunoprecipitation and affinity-binding studies revealed that Rab23 (show RAB23 Proteins) exists in a complex with Kif17 (show KIF17 Proteins) and importin b2 implying that Kif17 (show KIF17 Proteins) needs to bind to regulatory proteins like Rab23 (show RAB23 Proteins) for its ciliary transport
Association with Tnpo1 is necessary for Oxtr (show OXTR Proteins) nuclear localization. This is required for Oxt (show OXT Proteins)-induced osteoblast differentiation. osteoblast differentiation.
DJ-1 (show PARK7 Proteins) import is mediated by an oxidative stress-dependent interaction with karyopherin beta2.
Identification of a karyopherin beta1/beta2 proline-tyrosine nuclear localization signal in huntingtin (show HTT Proteins) protein.
Tnpo1 is involved in a variety of functions in the adult brain, including neurogenesis, cerebrospinal fluid production and sensing, and circadian rhythms.
This gene encodes the beta subunit of the karyopherin receptor complex which interacts with nuclear localization signals to target nuclear proteins to the nucleus. The karyopherin receptor complex is a heterodimer of an alpha subunit which recognizes the nuclear localization signal and a beta subunit which docks the complex at nucleoporins. Alternate splicing of this gene results in two transcript variants encoding different proteins.
M9 region interaction protein
, importin 2
, importin beta 2
, importin beta-2
, karyopherin (importin) beta 2
, karyopherin beta-2
, transportin 1
, major intrinsic protein of lens fiber 1