scholarly journals Structure, Dynamics, Evolution, and Function of a Major Scaffold Component in the Nuclear Pore Complex

Structure ◽  
2013 ◽  
Vol 21 (4) ◽  
pp. 560-571 ◽  
Author(s):  
Parthasarathy Sampathkumar ◽  
Seung Joong Kim ◽  
Paula Upla ◽  
William J. Rice ◽  
Jeremy Phillips ◽  
...  
Keyword(s):  
Nuclear Pore Complex ◽  
Nuclear Pore ◽  
Structure Dynamics ◽  
And Function

scholarly journals Structure, Dynamics, Evolution and Function of a Major Scaffold Component in the Nuclear Pore Complex

2014 ◽  
Vol 106 (2) ◽  
pp. 26a
Author(s):  
Seung Joong Kim ◽  
Parthasarathy Sampathkumar ◽  
Paula Upla ◽  
William Rice ◽  
Jeremy Phillips ◽  
...  
Keyword(s):  
Nuclear Pore Complex ◽  
Nuclear Pore ◽  
Structure Dynamics ◽  
And Function

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 NUP50 is necessary for the survival of primordial germ cells in mouse embryos

Reproduction ◽  
2016 ◽  
Vol 151 (1) ◽  
pp. 51-58 ◽  
Author(s):  
Eunsook Park ◽  
Bobae Lee ◽  
Bruce E Clurman ◽  
Keesook Lee
Keyword(s):  
Embryonic Development ◽  
Germ Cells ◽  
Nuclear Pore Complex ◽  
Essential Role ◽  
Primordial Germ Cells ◽  
Mouse Embryos ◽  
Nuclear Pore ◽  
Progressive Loss ◽  
And Function ◽  
Deficient Mice

Nucleoporin 50 kDa (NUP50), a component of the nuclear pore complex, is highly expressed in male germ cells, but its role in germ cells is largely unknown. In this study, we analyzed the expression and function of NUP50 during the embryonic development of germ cells using NUP50-deficient mice. NUP50 was expressed in germ cells of both sexes at embryonic day 15.5 (E15.5), E13.5, and E12.5. In addition, NUP50 expression was also detected in primordial germ cells (PGCs) migrating into the genital ridges at E9.5. The gonads of Nup50−/− embryos of both sexes contained few PGCs at both E11.5 and E12.5 and no developing germ cells at E15.5. The migratory PGCs in Nup50−/− embryos at E9.5 showed increased apoptosis but a normal rate of proliferation, resulting in the progressive loss of germ cells at later stages. Taken together, these results suggest that NUP50 plays an essential role in the survival of PGCs during embryonic development.

scholarly journals The role of the integral membrane nucleoporins Ndc1p and Pom152p in nuclear pore complex assembly and function

2006 ◽  
Vol 173 (3) ◽  
pp. 361-371 ◽  
Author(s):  
Alexis S. Madrid ◽  
Joel Mancuso ◽  
W. Zacheus Cande ◽  
Karsten Weis
Keyword(s):  
Electron Microscopy ◽  
Saccharomyces Cerevisiae ◽  
Nuclear Envelope ◽  
Lipid Bilayers ◽  
Nuclear Pore Complex ◽  
Transmembrane Proteins ◽  
Nuclear Pore ◽  
Large Channel ◽  
And Function

The nuclear pore complex (NPC) is a large channel that spans the two lipid bilayers of the nuclear envelope and mediates transport events between the cytoplasm and the nucleus. Only a few NPC components are transmembrane proteins, and the role of these proteins in NPC function and assembly remains poorly understood. We investigate the function of the three integral membrane nucleoporins, which are Ndc1p, Pom152p, and Pom34p, in NPC assembly and transport in Saccharomyces cerevisiae. We find that Ndc1p is important for the correct localization of nuclear transport cargoes and of components of the NPC. However, the role of Ndc1p in NPC assembly is partially redundant with Pom152p, as cells lacking both of these proteins show enhanced NPC disruption. Electron microscopy studies reveal that the absence of Ndc1p and Pom152p results in aberrant pores that have enlarged diameters and lack proteinaceous material, leading to an increased diffusion between the cytoplasm and the nucleus.

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