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Nup98 provides a scaffold for poised genes and mediates Induced enhancer-promoter contacts in genetic transcription.
Nup98 associates and colocalizes with the MBD (show DPEP1 Proteins)-R2/NSL and Trx (show GSR Proteins) complexes. Nup98 regulates transcription of Trx (show GSR Proteins) targets, the Hox (show MSH2 Proteins) genes.
Nup98, a virus-induced gene, was antiviral against a panel of viruses.
Study analyzed genomic interactions of full-length nucleoporins Nup98, Nup50 (show NUP50 Proteins), and Nup62 and found that they predominantly interacted with active genes inside the nucleoplasm, particularly those involved in developmental regulation and the cell cycle.
Nup88 (show NUP88 Proteins) localizes to silent loci, Sec13 (show SEC13 Proteins), Nup98, and a subset of FG-repeat nucleoporins bind to developmentally regulated genes undergoing transcription induction.
We demonstrated that Nup98-TopIIbeta and Nup98-SETBP1 (show SETBP1 Proteins) negatively regulate the XPO1 (show XPO1 Proteins)-mediated protein export. Our results will contribute to the understanding of the molecular mechanism by which the Nup98-fusion proteins induce tumorigenesis.
The age-associated accumulation of somatic mutations that occurs in the Nup98-HOXD13 (show HOXD13 Proteins) (NHD13) mouse model of leukemia progression was significantly elevated by co-expression of a PKR (show EIF2AK2 Proteins) transgene.
Nup50 (show NUP50 Proteins) dynamics are independent of importin alpha, Nup153 (show NUP153 Proteins), and Nup98, even though the latter two proteins also exhibit transcription-dependent mobility.
Data indicate that loss of cyclin-dependent kinase inhibitor p15 (p15Ink4b (show CDKN2B Proteins)) collaborates with oncogene (show RAB1A Proteins) fusion protein Nup98-HoxD13 (show HOXD13 Proteins) transgene in the development of predominantly myeloid neoplasms.
Homeobox (show PRRX1 Proteins) partners create more potent NUP98 fusion oncogenes than do non-homeobox (show PRRX1 Proteins) partners.
findings show that expression of NUP98-HOXD13 (show HOXD13 Proteins) impairs class switch recombination and reduces the antibody-mediated immune response, in addition to its role in leukemia
Mice expressing both the FLT3 (show FLT3 Proteins)/ITD and Nup98-HoxD13 (show HOXD13 Proteins) (NHD13) fusion gene developed acute myeloid leukemia (show BCL11A Proteins) with 100% penetrance
Data show that NUP98-HOXA10HD, a novel, canonical NUP98-Hox (show MSH2 Proteins) fusion, significantly enhances the self-renewal capacity of hematopoietic stem cells.
These results clearly demonstrate that Nup98 functions as a novel shuttling cofactor for Crm1 (show XPO1 Proteins)-mediated nuclear export in conjunction with RanBP3 (show RANBP3 Proteins).
A mouse model of CML blast crisis induced by cooperation between BCR/ABL (show ABL1 Proteins) and NUP98/HOXA9 (show HOXA9 Proteins)
data show that a novel nup98 was identified and it serves a role in nucleocytoplasmic trafficking similar to human NUP98.
The second FG repeat domain of the NUP98 moiety of the NUP98-HOXA9 (show HOXA9 Proteins) fusion protein is important for its cell immortalization and leukemogenesis activities. NUP98-HOXA9 (show HOXA9 Proteins) interacts with mixed lineage leukemia (MLL (show MLL Proteins)) via this FG repeat domain and that, in MLL (show MLL Proteins)-null mice, NUP98-HOXA9 (show HOXA9 Proteins)-induced cell immortalization and leukemogenesis are severely inhibited.
DYNLT1 (show DYNLT1 Proteins) interacts with nucleoporins and plays a role in the dysregulation of gene expression and induction of hematopoietic cell proliferation by the leukemogenic nucleoporin (show AGFG2 Proteins) fusion, NUP98-HOXA9 (show HOXA9 Proteins)
the mutation order in the NUP98-rearranged pediatric AML (show RUNX1 Proteins) begins with the NUP98 rearrangement leading to epigenetic dysregulations then followed by mutations of critical hematopoietic transcription factors and finally, activation of the FLT3 (show FLT3 Proteins) signaling pathway.
These results provide novel insight into the mechanisms underlying the aberrant capability of NUP98 oncoproteins to interact with APC (show APC Proteins)/C(Cdc20 (show CDC20 Proteins)) and to interfere with its function.
Our results suggest that NA10HD increases the number of gamma-globin-transduced HSCs that engraft, leading to an elevated number of fetal hemoglobin-containing red cells.
NUP98-HOXA9 (show HOXA9 Proteins) ability to induce blood cell expansion is evolutionarily conserved.
The study demonstrated the association of NUP98-IQCG with CRM1 (show XPO1 Proteins), and found that NUP98-IQCG expression inhibits the CRM1 (show XPO1 Proteins)-mediated nuclear export of p65 (show GORASP1 Proteins) and enhances the transcriptional activity of nuclear factor-kappaB. Moreover, IQCG could be entrapped in the nucleus by NUP98-IQCG, and the fusion protein interacts with calmodulin (show CALM1 Proteins) via the IQ motif in a calcium-independent manner.
The results indicate that highly selective targeting of Nup98-fusion proteins to Hox (show MSH2 Proteins) cluster regions via prebound Crm1 (show XPO1 Proteins) induces the formation of higher order chromatin structures that causes aberrant Hox (show MSH2 Proteins) gene regulation.
Despite the difference in localization, all tested Nup98 chimera provoked morphological alterations in the nuclear envelope (NE), in particular affecting the nuclear lamina and the lamina-associated polypeptide 2alpha.
NUP98-HOXA9 (show HOXA9 Proteins) expression induces myeloid disease.
These data support a model in which Nup98 interacts with microtubules and antagonizes MCAK (show KIF2C Proteins) activity, thus promoting bipolar spindle assembly.
Signal-mediated nuclear import and export proceed through the nuclear pore complex (NPC), which is comprised of approximately 50 unique proteins collectively known as nucleoporins. The 98 kDa nucleoporin is generated through a biogenesis pathway that involves synthesis and proteolytic cleavage of a 186 kDa precursor protein. This cleavage results in the 98 kDa nucleoporin as well as a 96 kDa nucleoporin, both of which are localized to the nucleoplasmic side of the NPC. Rat studies show that the 98 kDa nucleoporin functions as one of several docking site nucleoporins of transport substrates. The human gene has been shown to fuse to several genes following chromosome translocations in acute myelogenous leukemia (AML) and T-cell acute lymphocytic leukemia (T-ALL). This gene is one of several genes located in the imprinted gene domain of 11p15.5, an important tumor-suppressor gene region. Alterations in this region have been associated with the Beckwith-Wiedemann syndrome, Wilms tumor, rhabdomyosarcoma, adrenocortical carcinoma, and lung, ovarian, and breast cancer. Alternative splicing of this gene results in several transcript variants\; however, not all variants have been fully described.
, nucleoporin 98
, nucleoporin 98-96
, nucleoporin 98kD
, nucleoporin 98kDa
, nuclear pore complex protein Nup98-Nup96-like
, nuclear pore complex protein Nup98-Nup96
, 98 kDa nucleoporin
, nuclear pore complex protein Nup98
, nucleoporin Nup98
, GLFG-repeat containing nucleoporin