scholarly journals Structures of the autoproteolytic domain from the Saccharomyces cerevisiae nuclear pore complex component, Nup145

2010 ◽  
Vol 78 (8) ◽  
pp. 1992-1998 ◽  
Author(s):  
Parthasarathy Sampathkumar ◽  
Sinem A. Ozyurt ◽  
Johnny Do ◽  
Kevin T. Bain ◽  
Mark Dickey ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Nuclear Pore Complex ◽  
Nuclear Pore ◽  
Complex Component

scholarly journals GLE2, a Saccharomyces cerevisiae homologue of the Schizosaccharomyces pombe export factor RAE1, is required for nuclear pore complex structure and function.

1996 ◽  
Vol 7 (12) ◽  
pp. 1921-1937 ◽  
Author(s):  
R Murphy ◽  
J L Watkins ◽  
S R Wente
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Schizosaccharomyces Pombe ◽  
Nuclear Pore Complex ◽  
Nuclear Export ◽  
Protein Import ◽  
Nuclear Transport ◽  
Complex Structure ◽  
Striking Similarity ◽  
Nuclear Pore ◽  
Pore Complexes

To identify and characterize novel factors required for nuclear transport, a genetic screen was conducted in the yeast Saccharomyces cerevisiae. Mutations that were lethal in combination with a null allele of the gene encoding the nucleoporin Nup100p were isolated using a colony-sectoring assay. Three complementation groups of gle (for GLFG lethal) mutants were identified. In this report, the characterization of GLE2 is detailed. GLE2 encodes a 40.5-kDa polypeptide with striking similarity to that of Schizosaccharomyces pombe RAE1. In indirect immunofluorescence and nuclear pore complex fractionation experiments, Gle2p was associated with nuclear pore complexes. Mutated alleles of GLE2 displayed blockage of polyadenylated RNA export; however, nuclear protein import was not apparently diminished. Immunofluorescence and thin-section electron microscopic analysis revealed that the nuclear pore complex and nuclear envelope structure was grossly perturbed in gle2 mutants. Because the clusters of herniated pore complexes appeared subsequent to the export block, the structural perturbations were likely indirect consequences of the export phenotype. Interestingly, a two-hybrid interaction was detected between Gle2p and Srp1p, the nuclear localization signal receptor, as well as Rip1p, a nuclear export signal-interacting protein. We propose that Gle2p has a novel role in mediating nuclear transport.

scholarly journals Nuclear envelope-vacuole contacts mitigate nuclear pore complex assembly stress

2020 ◽  
Author(s):  
Christopher L. Lord ◽  
Susan R. Wente
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Nuclear Envelope ◽  
Nuclear Pore Complex ◽  
Lipid Droplets ◽  
Budding Yeast ◽  
Nuclear Transport ◽  
Nuclear Pore ◽  
Cellular Mechanisms ◽  
Complex Assembly ◽  
Cellular Effects

AbstractThe intricacy of nuclear pore complex (NPC) biogenesis imposes risks of failure that can cause defects in nuclear transport and nuclear envelope morphology, however, cellular mechanisms utilized to alleviate NPC assembly stress are not well-defined. In the budding yeast Saccharomyces cerevisiae, we demonstrate that NVJ1- and MDM1-enriched nuclear envelope (NE)-vacuole contacts increase when NPC assembly is compromised in several nup mutants, including nup116ΔGLFG cells. These interorganelle nucleus-vacuole junctions (NVJs) cooperate with lipid droplets to maintain viability and enhance NPC formation in assembly mutants. Additionally, NVJs function with ATG1 to promote vacuole-dependent remodeling in nup116ΔGLFG cells, which also correlates with proper NPC formation. Importantly, NVJs significantly improve the physiology of NPC assembly mutants, despite having only negligible effects when NPC biogenesis is unperturbed. Collectively, these results define how NE-vacuole interorganelle contacts coordinate responses to mitigate deleterious cellular effects caused by disrupted NPC assembly.SummaryHow cells respond to deleterious effects imposed by disrupted nuclear pore complex (NPC) assembly are not well-defined. The authors demonstrate nuclear envelope-vacuole interactions expand in response to perturbed NPC assembly to promote viability, nuclear envelope remodeling, and proper NPC biogenesis.

scholarly journals The FG-repeat asymmetry of the nuclear pore complex is dispensable for bulk nucleocytoplasmic transport in vivo

2004 ◽  
Vol 167 (4) ◽  
pp. 583-590 ◽  
Author(s):  
Bryan Zeitler ◽  
Karsten Weis
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Nuclear Pore Complex ◽  
Nucleocytoplasmic Transport ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Nucleocytoplasmic Trafficking ◽  
Transport Pathways ◽  
Pore Complexes ◽  
Biased Distribution

Nucleocytoplasmic transport occurs through gigantic proteinaceous channels called nuclear pore complexes (NPCs). Translocation through the NPC is exquisitely selective and is mediated by interactions between soluble transport carriers and insoluble NPC proteins that contain phenylalanine-glycine (FG) repeats. Although most FG nucleoporins (Nups) are organized symmetrically about the planar axis of the nuclear envelope, very few localize exclusively to one side of the NPC. We constructed Saccharomyces cerevisiae mutants with asymmetric FG repeats either deleted or swapped to generate NPCs with inverted FG asymmetry. The mutant Nups localize properly within the NPC and exhibit exchanged binding specificity for the export factor Xpo1. Surprisingly, we were unable to detect any defects in the Kap95, Kap121, Xpo1, or mRNA transport pathways in cells expressing the mutant FG Nups. These findings suggest that the biased distribution of FG repeats is not required for major nucleocytoplasmic trafficking events across the NPC.

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.

scholarly journals Crystal structure of human nuclear pore complex component NUP43

FEBS Letters ◽  
2015 ◽  
Vol 589 (21) ◽  
pp. 3247-3253 ◽  
Author(s):  
Chao Xu ◽  
Zhihong Li ◽  
Hao He ◽  
Amy Wernimont ◽  
Yanjun Li ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Nuclear Pore Complex ◽  
Nuclear Pore ◽  
Complex Component

scholarly journals The yeast nuclear pore complex functionally interacts with components of the spindle assembly checkpoint

2002 ◽  
Vol 159 (5) ◽  
pp. 807-819 ◽  
Author(s):  
Tatiana Iouk ◽  
Oliver Kerscher ◽  
Robert J. Scott ◽  
Munira A. Basrai ◽  
Richard W. Wozniak
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Cycle ◽  
Genetic Analysis ◽  
Nuclear Pore Complex ◽  
Spindle Assembly Checkpoint ◽  
Spindle Checkpoint ◽  
Spindle Assembly ◽  
Nuclear Pore ◽  
Yeast Saccharomyces Cerevisiae ◽  
Functional Link

Aphysical and functional link between the nuclear pore complex (NPC) and the spindle checkpoint machinery has been established in the yeast Saccharomyces cerevisiae. We show that two proteins required for the execution of the spindle checkpoint, Mad1p and Mad2p, reside predominantly at the NPC throughout the cell cycle. There they are associated with a subcomplex of nucleoporins containing Nup53p, Nup170p, and Nup157p. The association of the Mad1p–Mad2p complex with the NPC requires Mad1p and is mediated in part by Nup53p. On activation of the spindle checkpoint, we detect changes in the interactions between these proteins, including the release of Mad2p (but not Mad1p) from the NPC and the accumulation of Mad2p at kinetochores. Accompanying these events is the Nup53p-dependent hyperphosphorylation of Mad1p. On the basis of these results and genetic analysis of double mutants, we propose a model in which Mad1p bound to a Nup53p-containing complex sequesters Mad2p at the NPC until its release by activation of the spindle checkpoint. Furthermore, we show that the association of Mad1p with the NPC is not passive and that it plays a role in nuclear transport.

scholarly journals Nuclear Pore Complex Function in Saccharomyces cerevisiae Is Influenced by Glycosylation of the Transmembrane Nucleoporin Pom152p

Genetics ◽  
2005 ◽  
Vol 171 (3) ◽  
pp. 935-947 ◽  
Author(s):  
Kenneth D. Belanger ◽  
Amitabha Gupta ◽  
Kristy M. MacDonald ◽  
Christina M. Ott ◽  
Christine A. Hodge ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Nuclear Pore Complex ◽  
Complex Function ◽  
Nuclear Pore
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