Nuclear Pore Complex Protein Nup98

2020 ◽  
Author(s):  
Keyword(s):  
Nuclear Pore Complex ◽  
Nuclear Pore ◽  
Complex Protein

scholarly journals The Nuclear Pore Complex Protein Elys Is Required for Genome Stability in Mouse Intestinal Epithelial Progenitor Cells

2011 ◽  
Vol 140 (5) ◽  
pp. 1547-1555.e10 ◽  
Author(s):  
Nan Gao ◽  
Gangarao Davuluri ◽  
Weilong Gong ◽  
Christoph Seiler ◽  
Kristin Lorent ◽  
...  
Keyword(s):  
Progenitor Cells ◽  
Nuclear Pore Complex ◽  
Genome Stability ◽  
Nuclear Pore ◽  
Intestinal Epithelial ◽  
Complex Protein ◽  
Epithelial Progenitor Cells

scholarly journals A Small Ubiquitin-Related Polypeptide Involved in Targeting RanGAP1 to Nuclear Pore Complex Protein RanBP2

Cell ◽  
1997 ◽  
Vol 88 (1) ◽  
pp. 97-107 ◽  
Author(s):  
Rohit Mahajan ◽  
Christian Delphin ◽  
Tinglu Guan ◽  
Larry Gerace ◽  
Frauke Melchior
Keyword(s):  
Nuclear Pore Complex ◽  
Nuclear Pore ◽  
Complex Protein

scholarly journals Targeting and function in mRNA export of nuclear pore complex protein Nup153.

1996 ◽  
Vol 134 (5) ◽  
pp. 1141-1156 ◽  
Author(s):  
R Bastos ◽  
A Lin ◽  
M Enarson ◽  
B Burke
Keyword(s):  
Nuclear Pore Complex ◽  
Protein Import ◽  
Nucleocytoplasmic Transport ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Terminal Domain ◽  
General Decline ◽  
Complex Protein ◽  
Pore Complexes ◽  
And Function

Nup153 is a large (153 kD) O-linked glyco-protein which is a component of the basket structure located on the nucleoplasmic face of nuclear pore complexes. This protein exhibits a tripartite structure consisting of a zinc finger domain flanked by large (60-70 kD) NH2- and COOH-terminal domains. When full-length human Nup153 is expressed in BHK cells, it accumulates appropriately at the nucleoplasmic face of the nuclear envelope. Targeting information for Nup153 resides in the NH2-terminal domain since this region of the molecule can direct an ordinarily cytoplasmic protein, pyruvate kinase, to the nuclear face of the nuclear pore complex. Overexpression of Nup153 results in the dramatic accumulation of nuclear poly (A)+ RNA, suggesting an inhibition of RNA export from the nucleus. This is not due to a general decline in nucleocytoplasmic transport or to occlusion or loss of nuclear pore complexes since nuclear protein import is unaffected. While overexpression of certain Nup153 constructs was found to result in the formation of unusual intranuclear membrane arrays, this structural phenotype could not be correlated with the effects on poly (A)+ RNA distribution. The RNA trafficking defect was, however, dependent upon the Nup153 COOH-terminal domain which contains most of the XFXFG repeats. It is proposed that this region of Nup153, lying within the distal ring of the nuclear basket, represents a docking site for mRNA molecules exiting the nucleus.

scholarly journals GTP hydrolysis by Ran occurs at the nuclear pore complex in an early step of protein import.

1995 ◽  
Vol 131 (3) ◽  
pp. 571-581 ◽  
Author(s):  
F Melchior ◽  
T Guan ◽  
N Yokoyama ◽  
T Nishimoto ◽  
L Gerace
Keyword(s):  
Nuclear Pore Complex ◽  
Nuclear Import ◽  
Protein Import ◽  
Small Gtpase ◽  
Nuclear Pore ◽  
Binding Studies ◽  
Early Step ◽  
Permeabilized Cells ◽  
Complex Protein ◽  
Ran Gtp

Mediated import of proteins into the nucleus involves multiple cytosolic factors, including the small GTPase Ran. Whether Ran functions by interacting with other cytosolic proteins or components of the nuclear pore complex has been unclear. Furthermore, the precise transport step where Ran acts has not been determined. To address these questions, we have analyzed the binding interactions of Ran using permeabilized cells and isolated nuclear envelopes. By light and electron microscope immunolocalization, we have found that Ran accumulates specifically at the cytoplasmic surface of the nuclear pore complex when nuclear import in permeabilized cells is inhibited by nonhydrolyzable analogs of GTP. Ran associates with a peripheral pore complex region that is similar to the area where transport ligands accumulate by depletion of ATP, which arrests an early step of transport. Binding studies with isolated nuclear envelopes in the absence of added cytosol indicate that Ran-GTP directly interacts with a pore complex protein. Using blot overlay techniques, we detected a single prominent polypeptide of isolated nuclear envelopes that binds Ran-GTP. This corresponds to the 358-kD protein RanBP2, a Ran binding pore complex protein recently identified by two-hybrid screening. Thus, RanBP2 is likely to constitute the Ran-GTP-binding site detected at the cytoplasmic periphery of the pore complex. These data support a model in which initial ligand binding to the nuclear pore complex occurs at or near RanBP2, and that hydrolysis of GTP by Ran at this site serves to define commitment to the nuclear import pathway.

The nuclear pore complex protein ALADIN is anchored via NDC1 but not via POM121 and GP210 in the nuclear envelope

2009 ◽  
Vol 390 (2) ◽  
pp. 205-210 ◽  
Author(s):  
Barbara Kind ◽  
Katrin Koehler ◽  
Mike Lorenz ◽  
Angela Huebner
Keyword(s):  
Nuclear Envelope ◽  
Nuclear Pore Complex ◽  
Nuclear Pore ◽  
Complex Protein

Sequence analysis of a cDNA encoding a human nuclear pore complex protein, hnup153

1994 ◽  
Vol 1217 (2) ◽  
pp. 219-223 ◽  
Author(s):  
Isabel McMorrow ◽  
Ricardo Bastos ◽  
Heidi Horton ◽  
Brian Burke
Keyword(s):  
Sequence Analysis ◽  
Nuclear Pore Complex ◽  
Nuclear Pore ◽  
Complex Protein

scholarly journals Nup2 performs diverse interphase functions inAspergillus nidulans

2018 ◽  
Vol 29 (26) ◽  
pp. 3144-3154 ◽  
Author(s):  
Subbulakshmi Suresh ◽  
Sarine Markossian ◽  
Aysha H. Osmani ◽  
Stephen A. Osmani
Keyword(s):  
Nuclear Pore Complex ◽  
Nuclear Import ◽  
Nuclear Proteins ◽  
Nuclear Accumulation ◽  
Nuclear Pore ◽  
Nuclear Movement ◽  
Multifunctional Protein ◽  
Long Period ◽  
Complex Protein ◽  
Mitotic Chromatin

The nuclear pore complex (NPC) protein Nup2 plays interphase nuclear transport roles and in Aspergillus nidulans also functions to bridge NPCs at mitotic chromatin for their faithful coinheritance to daughter G1 nuclei. In this study, we further investigate the interphase functions of Nup2 in A. nidulans. Although Nup2 is not required for nuclear import of all nuclear proteins after mitosis, it is required for normal G1 nuclear accumulation of the NPC nuclear basket–associated components Mad2 and Mlp1 as well as the THO complex protein Tho2. Targeting of Mlp1 to nuclei partially rescues the interphase delay seen in nup2 mutants indicating that some of the interphase defects in Nup2-deleted cells are due to Mlp1 mislocalization. Among the inner nuclear membrane proteins, Nup2 affects the localization of Ima1, orthologues of which are involved in nuclear movement. Interestingly, nup2 mutant G1 nuclei also exhibit an abnormally long period of extensive to-and-fro movement immediately after mitosis in a manner dependent on the microtubule cytoskeleton. This indicates that Nup2 is required to limit the transient postmitotic nuclear migration typical of many filamentous fungi. The findings reveal that Nup2 is a multifunctional protein that performs diverse functions during both interphase and mitosis in A. nidulans.

scholarly journals Nuclear Pore Complex Protein Mediated Nuclear Localization of Dicer Protein in Human Cells

PLoS ONE ◽  
2011 ◽  
Vol 6 (8) ◽  
pp. e23385 ◽  
Author(s):  
Yoshinari Ando ◽  
Yasuhiro Tomaru ◽  
Ayako Morinaga ◽  
Alexander Maxwell Burroughs ◽  
Hideya Kawaji ◽  
...  
Keyword(s):  
Nuclear Localization ◽  
Nuclear Pore Complex ◽  
Human Cells ◽  
Nuclear Pore ◽  
Complex Protein ◽  
Dicer Protein
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