-
high-affinity binding of karyopherin-beta2 to the FUS C-terminal proline-tyrosine nuclear localization signal tethers the proteins together, allowing multiple, distributed weak intermolecular contacts to disrupt FUS self-association, blocking liquid-liquid phase separation
-
TNPO1-mediated nuclear import may constitute a novel input pathway of how cellular redox state signals to the clock, since redox stress increases binding of TNPO1 to PER1 and decreases its nuclear localization. TNPO1 is one of the novel players essential for normal circadian periods and potentially for redox regulation of the clock.
-
A molecular docking and dynamics study concluded that R521C and R521H mutations in FUS result in weak binding with Karyopherin-beta2 leading to amyotrophic lateral sclerosis.
-
Data suggest that micoRNA-128 targets the 3prime-untranslated region of nuclear import factor transportin 1 (TNPO1) mRNA.
-
the TNPO1-Rab8-ciliary targeting signals complex mediates selective entry into and retention of cargos within cilia.
-
Together, these results indicate that transportin-1 mediates YB-1 nuclear translocation.
-
findings suggest that a new player, i.e., O-GlcNAcylation, regulates hnRNP A1 translocation and interaction with Trn1, possibly affecting its function
-
Importins, Impbeta, Kapbeta2, Imp4, Imp5, Imp7, Imp9, and Impalpha, show the H3 tail binding more tightly than the H4 tail. The H3 tail binds Kapbeta2 and Imp5 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 with high affinity even though H3 lacks a recognizable proline-tyrosine nuclear localization signal (PY-NLS).
-
FGF2 nuclear translocation is regulated by Karyopherin-beta2 and Ran GTPase in human glioblastoma cells
-
Kapbeta2 interacts with ULK2 through ULK2's putative PY-NLS motif, and facilitates transport from the cytoplasm to the nucleus, depending on its Ser1027 residue phosphorylation by PKA, thereby reducing autophagic activity.
-
Studies indicate potential roles of Tranportin-1 and Transportin-2 beyond protein nuclear import.
-
ADAR1 carries a unique nuclear localization signal (NLS) that overlaps one of its double-stranded RNA-binding domains (dsRBDs). This dsRBD-NLS is recognized by nuclear import receptor transportin 1 (also called karyopherin-beta2) in an RNA-sensitive manner.
-
Data suggest the C-terminal nuclear localization domain (QYP) is critical for RAM (RNMT-activating mini protein) to enter the cell nucleus where RAM activates RNMT resulting in mRNA cap methylation; TNPO1/TNPO2 mediate RAM nuclear entry.
-
C-terminal FUS mutations prevent TNPO 1 binding to the NLS, inhibiting nuclear import and promoting cytoplasmic aggregation. The presence of TNPO 1 in wild-type FUS aggregates in frontotemporal lobar degeneration-FUS distinguishes it from ALS.
-
Crystal structure of human Karyopherin beta2 bound to the PY-NLS of Saccharomyces cerevisiae Nab2
-
The crystal structure of the FUS-NLS/Trn1 complex shows extensive contacts between the two proteins and a unique alpha-helical structure in the FUS-NLS.
-
Disulfide formation with transportin-1 is required for nuclear localization and the activation of FOXO4 induced by reactive oxygen species.
-
In case of L7, importin beta2 or importin beta3 are preferentially used by clusters with a high import efficiency.
-
These data imply a specific dysfunction in the interaction between Trn1 and FET proteins in the inclusion body formation in FTLD-FUS.
