| Human RTEL1 Interacts with KPNB1 (Importin beta) and NUP153 and Connects Nuclear Import to Nuclear Envelope Stability in S-Phase. | Human RTEL1 Interacts with KPNB1 (Importin β) and NUP153 and Connects Nuclear Import to Nuclear Envelope Stability in S-Phase.
Schertzer M, Jullien L, Pinto AL, Calado RT, Revy P, Londoño-Vallejo A., Free PMC Article | 01/3/2024 |
| NUP153 promotes HCC cells proliferation via c-Myc-mediated downregulation of P15[INK4b]. | NUP153 promotes HCC cells proliferation via c-Myc-mediated downregulation of P15(INK4b).
Gan C, Zhou K, Li M, Shang J, Liu L, Zhao Q. | 12/3/2022 |
| Defining the HIV Capsid Binding Site of Nucleoporin 153. | Defining the HIV Capsid Binding Site of Nucleoporin 153.
Li S, Patel JS, Yang J, Crabtree AM, Rubenstein BM, Lund-Andersen PK, Ytreberg FM, Rowley PA., Free PMC Article | 11/5/2022 |
| Viral protein X unlocks the nuclear pore complex through a human Nup153-dependent pathway to promote nuclear translocation of the lentiviral genome. | Viral protein X unlocks the nuclear pore complex through a human Nup153-dependent pathway to promote nuclear translocation of the lentiviral genome.
Singh SP, Raja S, Mahalingam S., Free PMC Article | 12/5/2020 |
| Seh1 is not required for the association of the Nup107 complex with mitotic chromosomes, but it is essential for the association of both the GATOR2 complex and nucleoporin Nup153 with mitotic chromosomes. | Seh1 targets GATOR2 and Nup153 to mitotic chromosomes.
Platani M, Samejima I, Samejima K, Kanemaki MT, Earnshaw WC., Free PMC Article | 12/7/2019 |
| Nup153 effectively assembled Nup98, Nup62 and Pom121 of the nuclear pore complex at the end of the mitosis. | Roles of Nup133, Nup153 and membrane fenestrations in assembly of the nuclear pore complex at the end of mitosis.
Bilir Ş, Kojidani T, Mori C, Osakada H, Kobayashi S, Koujin T, Hiraoka Y, Haraguchi T. | 06/1/2019 |
| Nup153 is essential for the HIV-1 nuclear import in nondividing cells, and CPSF6 is important for HIV-1 integration. | Nup153 Unlocks the Nuclear Pore Complex for HIV-1 Nuclear Translocation in Nondividing Cells.
Buffone C, Martinez-Lopez A, Fricke T, Opp S, Severgnini M, Cifola I, Petiti L, Frabetti S, Skorupka K, Zadrozny KK, Ganser-Pornillos BK, Pornillos O, Di Nunzio F, Diaz-Griffero F., Free PMC Article | 09/22/2018 |
| Despite the requirement of all three nucleoporins for accurate NHEJ, only Nup153 is needed for proper nuclear import of 53BP1 and SENP1-dependent sumoylation of 53BP1. Our data support the role of Nup153 as an important regulator of 53BP1 activity and efficient NHEJ. | Localisation of Nup153 and SENP1 to nuclear pore complexes is required for 53BP1-mediated DNA double-strand break repair.
Duheron V, Nilles N, Pecenko S, Martinelli V, Fahrenkrog B. | 09/15/2018 |
| results further highlight the antagonistic relationship between 53BP1 and BRCA1, and place Nup153 and Nup50 in a molecular pathway that regulates 53BP1 function by counteracting BRCA1-mediated events. | Nup153 and Nup50 promote recruitment of 53BP1 to DNA repair foci by antagonizing BRCA1-dependent events.
Mackay DR, Howa AC, Werner TL, Ullman KS. | 05/26/2018 |
| Nup153 is an epigenetic regulator which, upon altered NO signalling, mediates the activation of genes potentially associated with early dystrophic cardiac remodelling. | The nuclear pore protein Nup153 associates with chromatin and regulates cardiac gene expression in dystrophic mdx hearts.
Nanni S, Re A, Ripoli C, Gowran A, Nigro P, D'Amario D, Amodeo A, Crea F, Grassi C, Pontecorvi A, Farsetti A, Colussi C. | 01/20/2018 |
| NUP153 and CPSF6 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. | Host cofactors and pharmacologic ligands share an essential interface in HIV-1 capsid that is lost upon disassembly.
Price AJ, Jacques DA, McEwan WA, Fletcher AJ, Essig S, Chin JW, Halambage UD, Aiken C, James LC., Free PMC Article | 04/30/2016 |
| 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 | Kirkwood-Buff Approach Rescues Overcollapse of a Disordered Protein in Canonical Protein Force Fields.
Mercadante D, Milles S, Fuertes G, Svergun DI, Lemke EA, Gräter F. | 04/2/2016 |
| 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. | Structural characterization of altered nucleoporin Nup153 expression in human cells by thin-section electron microscopy.
Duheron V, Chatel G, Sauder U, Oliveri V, Fahrenkrog B., Free PMC Article | 09/26/2015 |
| Nucleoporin Nup153 is required for NPC assembly during interphase but not during mitotic exit. It functions in interphasic NPC formation by binding directly to the inner nuclear membrane via an N-terminal amphipathic helix. | Nup153 Recruits the Nup107-160 Complex to the Inner Nuclear Membrane for Interphasic Nuclear Pore Complex Assembly.
Vollmer B, Lorenz M, Moreno-Andrés D, Bodenhöfer M, De Magistris P, Astrinidis SA, Schooley A, Flötenmeyer M, Leptihn S, Antonin W. | 08/29/2015 |
| The data presented here suggest that BGLF4 interferes with the normal functions of Nup62 and Nup153 and preferentially helps the nuclear import of viral proteins for viral DNA replication and assembly. | BGLF4 kinase modulates the structure and transport preference of the nuclear pore complex to facilitate nuclear import of Epstein-Barr virus lytic proteins.
Chang CW, Lee CP, Su MT, Tsai CH, Chen MR., Free PMC Article | 04/11/2015 |
| These data reveal an emergent Kap-centric barrier mechanism that may underlie mechanistic and kinetic control in the nuclear pore complex. | Karyopherin-centric control of nuclear pores based on molecular occupancy and kinetic analysis of multivalent binding with FG nucleoporins.
Kapinos LE, Schoch RL, Wagner RS, Schleicher KD, Lim RY., Free PMC Article | 12/6/2014 |
| a subset of lentiviral CA proteins directly engage FG-motifs present on NUP153 to affect viral nuclear import. | Nucleoporin NUP153 phenylalanine-glycine motifs engage a common binding pocket within the HIV-1 capsid protein to mediate lentiviral infectivity.
Matreyek KA, Yücel SS, Li X, Engelman A., Free PMC Article | 05/31/2014 |
| The Nup153 binds to both SENP1 and SENP2 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. | Two distinct sites in Nup153 mediate interaction with the SUMO proteases SENP1 and SENP2.
Chow KH, Elgort S, Dasso M, Ullman KS., Free PMC Article | 05/17/2014 |
| 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 and Nup153. | Nuclear import of cutaneous beta genus HPV8 E7 oncoprotein is mediated by hydrophobic interactions between its zinc-binding domain and FG nucleoporins.
Onder Z, Moroianu J., Free PMC Article | 04/12/2014 |
| The roles of NUP153 and nup98 in the integration and replication of HIV-1 in human Jurkat lymphocytes are reported. | Nup153 and Nup98 bind the HIV-1 core and contribute to the early steps of HIV-1 replication.
Di Nunzio F, Fricke T, Miccio A, Valle-Casuso JC, Perez P, Souque P, Rizzi E, Severgnini M, Mavilio F, Charneau P, Diaz-Griffero F., Free PMC Article | 06/15/2013 |
| analysis of the Nup153-Nup50 protein interface and its role in nuclear import | The Nup153-Nup50 protein interface and its role in nuclear import.
Makise M, Mackay DR, Elgort S, Shankaran SS, Adam SA, Ullman KS., Free PMC Article | 02/2/2013 |
| human nucleoporin 153 (NUP153) has a role in repair of DSBs and in the activation of DNA damage checkpoints. | The nucleoporin 153, a novel factor in double-strand break repair and DNA damage response.
Lemaître C, Fischer B, Kalousi A, Hoffbeck AS, Guirouilh-Barbat J, Shahar OD, Genet D, Goldberg M, Betrand P, Lopez B, Brino L, Soutoglou E. | 01/26/2013 |
| Nup153 binds to importin alpha | The interaction between importin-α and Nup153 promotes importin-α/β-mediated nuclear import.
Ogawa Y, Miyamoto Y, Oka M, Yoneda Y. | 10/6/2012 |
| Data show that the C-terminal part of NUP153 is required for effective 53BP1 nuclear import, and that 53BP1 is imported to the nucleus through the NUP153-importin-beta interplay. | Nucleoporin NUP153 guards genome integrity by promoting nuclear import of 53BP1.
Moudry P, Lukas C, Macurek L, Neumann B, Heriche JK, Pepperkok R, Ellenberg J, Hodny Z, Lukas J, Bartek J., Free PMC Article | 08/18/2012 |
| Nup153 levels regulate the localization of Mad1 during the metaphase/anaphase transition thereby affecting its phoshorylation status and in turn spindle checkpoint activity and mitotic exit. | The nucleoporin Nup153 affects spindle checkpoint activity due to an association with Mad1.
Lussi YC, Shumaker DK, Shimi T, Fahrenkrog B., Free PMC Article | 06/30/2012 |