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Nup153 and Megator (Mtor (show FRAP1 Proteins)) bind to 25% of the genome in continuous domains extending 10 kb to 500 kb.
The FG repeats of Nup153 are necessary for its function in transport, whereas the remainder of the protein maintains pore integrity.
Nup50 (show NUP50 Proteins) dynamics are independent of importin alpha, Nup153, and Nup98 (show NUP98 Proteins), even though the latter two proteins also exhibit transcription-dependent mobility.
results demonstrate a chromatin-associated role of Nup153 in maintaining stem cell pluripotency by functioning in mammalian epigenetic gene silencing
Nup153 is an epigenetic regulator which, upon altered NO signalling, mediates the activation of genes potentially associated with early dystrophic cardiac remodelling.
NUP153 and CPSF6 (show CPSF6 Proteins) have overlapping binding sites, but each makes unique capsid monomers (CA) interactions. Multiple ligands share an overlapping interface in HIV-1 capsid that is lost upon viral disassembly.
Study assessed the extent of collapse of a Nup153 fragment in molecular dynamics simulations and compared the results to single molecule FRET and small-angle X-ray scattering experiments of this peptide
Our data indicate a central function of Nup153 in the organization of the nucleus, not only at the periphery, but throughout the entire nuclear interior.
Nucleoporin Nup153 is required for NPC (show NPC1 Proteins) assembly during interphase but not during mitotic exit. It functions in interphasic NPC (show NPC1 Proteins) formation by binding directly to the inner nuclear membrane via an N-terminal amphipathic helix.
The data presented here suggest that BGLF4 interferes with the normal functions of Nup62 (show NUP62 Proteins) and Nup153 and preferentially helps the nuclear import of viral proteins for viral DNA replication and assembly.
These data reveal an emergent Kap (show CDKN3 Proteins)-centric barrier mechanism that may underlie mechanistic and kinetic control in the nuclear pore complex.
a subset of lentiviral CA proteins directly engage FG-motifs present on NUP153 to affect viral nuclear import.
The Nup153 binds to both SENP1 (show SENP1 Proteins) and SENP2 (show SUMO1 Proteins) and does so by interacting with the unique N-terminal domain of Nup153 as well as a specific region within the C-terminal FG-rich region.
A hydrophobic patch 65LRLFV69 within the zinc-binding domain is essential for the nuclear import and localization of HPV8 E7 via hydrophobic interactions with Nup62 (show NUP62 Proteins) and Nup153.
analysis of RNA recognition sequence preference by the nucleoporin Nup153
Nuclear pore complexes are extremely elaborate structures that mediate the regulated movement of macromolecules between the nucleus and cytoplasm. These complexes are composed of at least 100 different polypeptide subunits, many of which belong to the nucleoporin family. Nucleoporins are pore complex-specific glycoproteins characterized by cytoplasmically oriented O-linked N-acetylglucosamine residues and numerous repeats of the pentapeptide sequence XFXFG. The protein encoded by this gene has three distinct domains: a N-terminal region within which a pore targeting domain has been identified, a central region containing multiple zinc finger motifs, and a C-terminal region containing multiple XFXFG repeats.
, nucleoporin 153
, nuclear pore complex protein Nup153
, nucleoporin 153kDa
, nuclear pore complex protein Nup153-like
, 153 kDa nucleoporin
, nucleoporin 153kD
, nucleoporin Nup153
, nuclear pore complex protein hnup153