scholarly journals NSF- and SNARE-mediated membrane fusion is required for nuclear envelope formation and completion of nuclear pore complex assembly in Xenopus laevis egg extracts

2007 ◽  
Vol 120 (16) ◽  
pp. 2895-2903 ◽  
Author(s):  
T. Baur ◽  
K. Ramadan ◽  
A. Schlundt ◽  
J. Kartenbeck ◽  
H. H. Meyer
Keyword(s):  
Xenopus Laevis ◽  
Nuclear Envelope ◽  
Membrane Fusion ◽  
Nuclear Pore Complex ◽  
Nuclear Pore ◽  
Complex Assembly ◽  
Egg Extracts ◽  
Nuclear Envelope Formation

Concentration of Ran on chromatin induces decondensation, nuclear envelope formation and nuclear pore complex assembly

2002 ◽  
Vol 81 (11) ◽  
pp. 623-633 ◽  
Author(s):  
Chuanmao Zhang ◽  
Martin W. Goldberg ◽  
William J. Moore ◽  
Terence D. Allen ◽  
Paul R. Clarke
Keyword(s):  
Nuclear Envelope ◽  
Nuclear Pore Complex ◽  
Nuclear Pore ◽  
Complex Assembly ◽  
Nuclear Envelope Formation

scholarly journals The Integral Membrane Nucleoporin pom121 Functionally Links Nuclear Pore Complex Assembly and Nuclear Envelope Formation

2005 ◽  
Vol 17 (1) ◽  
pp. 83-92 ◽  
Author(s):  
Wolfram Antonin ◽  
Cerstin Franz ◽  
Uta Haselmann ◽  
Claude Antony ◽  
Iain W. Mattaj
Keyword(s):  
Nuclear Envelope ◽  
Nuclear Pore Complex ◽  
Nuclear Pore ◽  
Complex Assembly ◽  
Nuclear Envelope Formation

scholarly journals Regulation and coordination of nuclear envelope and nuclear pore complex assembly

Nucleus ◽  
2013 ◽  
Vol 4 (2) ◽  
pp. 105-114 ◽  
Author(s):  
Michaela Clever ◽  
Yasuhiro Mimura ◽  
Tomoko Funakoshi ◽  
Naoko Imamoto
Keyword(s):  
Nuclear Envelope ◽  
Nuclear Pore Complex ◽  
Nuclear Pore ◽  
Complex Assembly

scholarly journals Piecing together nuclear pore complex assembly during interphase

2009 ◽  
Vol 185 (3) ◽  
pp. 377-379 ◽  
Author(s):  
Michael Rexach
Keyword(s):  
Nuclear Envelope ◽  
Nuclear Pore Complex ◽  
Supramolecular Structures ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Assembly Process ◽  
Nuclear Pores ◽  
Complex Assembly ◽  
Cell Biol ◽  
Pore Complexes

All nucleocytoplasmic traffic of macromolecules occurs through nuclear pore complexes (NPCs), which function as stents in the nuclear envelope to keep nuclear pores open but gated. Three studies in this issue (Flemming, D., P. Sarges, P. Stelter, A. Hellwig, B. Böttcher, and E. Hurt. 2009. J. Cell Biol. 185:387–395; Makio, T., L.H. Stanton, C.-C. Lin, D.S. Goldfarb, K. Weis, and R.W. Wozniak. 2009. J. Cell Biol. 185:459–491; Onishchenko, E., L.H. Stanton, A.S. Madrid, T. Kieselbach, and K. Weis. 2009. J. Cell Biol. 185:475–491) further our understanding of the NPC assembly process by reporting what happens when the supply lines of key proteins that provide a foundation for building these marvelous supramolecular structures are disrupted.

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.

Dimples, pores, star-rings, and thin rings on growing nuclear envelopes: evidence for structural intermediates in nuclear pore complex assembly

1997 ◽  
Vol 110 (4) ◽  
pp. 409-420 ◽  
Author(s):  
M.W. Goldberg ◽  
C. Wiese ◽  
T.D. Allen ◽  
K.L. Wilson
Keyword(s):  
Nuclear Pore Complex ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Complex Assembly ◽  
Egg Extracts ◽  
High Concentrations ◽  
Pore Complexes ◽  
Xenopus Egg Extracts

We used field emission in-lens scanning electron microscopy to examine newly-assembled, growing nuclear envelopes in Xenopus egg extracts. Scattered among nuclear pore complexes were rare ‘dimples’ (outer membrane depressions, 5–35 nm diameter), more abundant holes (pores) with a variety of edge geometries (35–45 nm diameter; 3.3% of structures), pores containing one to eight triangular ‘star-ring’ subunits (2.1% of total), and more complicated structures. Neither mature complexes, nor these novel structures, formed when wheat germ agglutinin (which binds O-glycosylated nucleoporins) was added at high concentrations (>500 microg/ml) directly to the assembly reaction; low concentrations (10 microg/ml) had no effect. However at intermediate concentrations (50–100 microg/ml), wheat germ agglutinin caused a dramatic, sugar-reversible accumulation of ‘empty’ pores, and other structures; this effect correlated with the lectin-induced precipitation of a variable proportion of each major Xenopus wheat-germ-agglutinin-binding nucleoporin. Another inhibitor, dibromo-BAPTA (5,5′-dibromo-1,2-bis[o-aminophenoxylethane-N,N,N′,N′-tetraacetic acid), had different effects depending on its time of addition to the assembly reaction. When 1 mM dibromo-BAPTA was added at time zero, no pore-related structures formed. However, when dibromo-BAPTA was added to growing nuclei 40–45 minutes after initiating assembly, star-rings and other structures accumulated, suggesting that dibromo-BAPTA can inhibit multiple stages in pore complex assembly. We propose that assembly begins with the formation and stabilization of a hole (pore) through the nuclear envelope, and that dimples, pores, star-rings, and thin rings are structural intermediates in nuclear pore complex assembly.

Yeast Nuclear Pore Complex Assembly Defects Determined by Nuclear Envelope Reconstruction

2000 ◽  
Vol 132 (1) ◽  
pp. 1-5 ◽  
Author(s):  
Natalia Gomez-Ospina ◽  
Garry Morgan ◽  
Thomas H. Giddings ◽  
Buket Kosova ◽  
Ed Hurt ◽  
...  
Keyword(s):  
Nuclear Envelope ◽  
Nuclear Pore Complex ◽  
Nuclear Pore ◽  
Complex Assembly ◽  
Envelope Reconstruction

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

2020 ◽  
Vol 219 (12) ◽  
Author(s):  
Christopher L. Lord ◽  
Susan R. Wente
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Nuclear Envelope ◽  
Nuclear Pore Complex ◽  
Lipid Droplets ◽  
Budding Yeast ◽  
Nuclear Pore ◽  
Cellular Mechanisms ◽  
Yeast Saccharomyces Cerevisiae ◽  
Complex Assembly ◽  
Cellular Effects

The intricacy of nuclear pore complex (NPC) biogenesis imposes risks of failure that can cause defects in nuclear transport and nuclear envelope (NE) morphology; however, cellular mechanisms used to alleviate NPC assembly stress are not well defined. In the budding yeast Saccharomyces cerevisiae, we demonstrate that NVJ1- and MDM1-enriched 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 remodel the NE and promote vacuole-dependent degradation of specific nucleoporins in nup116ΔGLFG cells. Importantly, NVJs significantly improve the physiology of NPC assembly mutants, despite having only negligible effects when NPC biogenesis is unperturbed. These results therefore define how NE–vacuole interorganelle contacts coordinate responses to mitigate deleterious cellular effects caused by disrupted NPC assembly.

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