Faculty Opinions recommendation of Chromatin boundaries in budding yeast: the nuclear pore connection.

2002 ◽  
Author(s):  
Pamela Geyer
Keyword(s):  
Budding Yeast ◽  
Nuclear Pore

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 In vivo single-particle imaging of nuclear mRNA export in budding yeast demonstrates an essential role for Mex67p

2015 ◽  
Vol 211 (6) ◽  
pp. 1121-1130 ◽  
Author(s):  
Carlas Smith ◽  
Azra Lari ◽  
Carina Patrizia Derrer ◽  
Anette Ouwehand ◽  
Ammeret Rossouw ◽  
...  
Keyword(s):  
Single Particle ◽  
Messenger Rna ◽  
Essential Role ◽  
Budding Yeast ◽  
Retrograde Transport ◽  
Nuclear Pore ◽  
Messenger Ribonucleoprotein ◽  
Particle Imaging ◽  
Single Particle Imaging

Many messenger RNA export proteins have been identified; yet the spatial and temporal activities of these proteins and how they determine directionality of messenger ribonucleoprotein (mRNP) complex export from the nucleus remain largely undefined. Here, the bacteriophage PP7 RNA-labeling system was used in Saccharomyces cerevisiae to follow single-particle mRNP export events with high spatial precision and temporal resolution. These data reveal that mRNP export, consisting of nuclear docking, transport, and cytoplasmic release from a nuclear pore complex (NPC), is fast (∼200 ms) and that upon arrival in the cytoplasm, mRNPs are frequently confined near the nuclear envelope. Mex67p functions as the principal mRNP export receptor in budding yeast. In a mex67-5 mutant, delayed cytoplasmic release from NPCs and retrograde transport of mRNPs was observed. This proves an essential role for Mex67p in cytoplasmic mRNP release and directionality of transport.

scholarly journals Nuclear Export Through Nuclear Envelope Remodeling inSaccharomyces cerevisiae

2017 ◽  
Author(s):  
Baojin Ding ◽  
Anne M. Mirza ◽  
James Ashley ◽  
Vivian Budnik ◽  
Mary Munson
Keyword(s):  
Nuclear Envelope ◽  
Nuclear Export ◽  
Mammalian Cells ◽  
Budding Yeast ◽  
Mrna Export ◽  
Low Frequency ◽  
Nuclear Pore ◽  
Wild Type ◽  
Export Pathway ◽  
Wild Type Yeast

ABSTRACTIn eukaryotes, subsets of exported mRNAs are organized into large ribonucleoprotein (megaRNP) granules. How megaRNPs exit the nucleus is unclear, as their diameters are much larger than the nuclear pore complex (NPC) central channel. We previously identified a non-canonical nuclear export mechanism inDrosophila(Speese et al.,Cell2012) and mammals (Ding et al., in preparation), in which megaRNPs exit the nucleus by budding across nuclear envelope (NE) membranes. Here, we present evidence for a similar pathway in the nucleus of the budding yeast S.cerevisiae, which contain morphologically similar granules bearing mRNAs. Wild-type yeast displayed these granules at very low frequency, but this frequency was dramatically increased when the non-essential NPC protein Nup116 was deleted. These granules were not artifacts of defective NPCs; a mutation in the exportinXPO1(CRM1), in which NPCs are normal, induced similar megaRNP upregulation. We hypothesize that a non-canonical nuclear export pathway, analogous to those observed inDrosophilaand in mammalian cells, exists in yeast, and that this pathway is upregulated for use when NPCs or nuclear export are impaired.SUMMARYDing et al., describe a non-canonical mRNA export pathway in budding yeast similar to that observed inDrosophila. This pathway appears upregulated when the NPC is impaired, nuclear envelope integrity is disrupted, or the export factor Xpo1 (CRM1) is defective.

scholarly journals Adding complexity to the nuclear pore complex

2015 ◽  
Vol 208 (6) ◽  
pp. 651-651
Author(s):  
Ben Short
Keyword(s):  
Nuclear Pore Complex ◽  
Budding Yeast ◽  
Muscle Differentiation ◽  
Nuclear Pore

Two studies describe how nucleoporins affect muscle differentiation and budding yeast lifespan.

scholarly journals Meiotic Cellular Rejuvenation is Coupled to Nuclear Remodeling in Budding Yeast

2019 ◽  
Author(s):  
Grant A. King ◽  
Jay S. Goodman ◽  
Keerthana Chetlapalli ◽  
Jennifer G. Schick ◽  
Danielle M. Jorgens ◽  
...  
Keyword(s):  
Quality Control ◽  
De Novo ◽  
Budding Yeast ◽  
Time Lapse ◽  
Cellular Damage ◽  
Nuclear Pore ◽  
The Core ◽  
Nucleolar Material ◽  
Nuclear Remodeling ◽  
Insight Into

ABSTRACTProduction of healthy gametes in meiosis relies on the quality control and proper distribution of both nuclear and cytoplasmic contents. Meiotic differentiation naturally eliminates age-induced cellular damage by an unknown mechanism. Using time-lapse fluorescence microscopy in budding yeast, we found that nuclear senescence factors – including protein aggregates, extrachromosomal ribosomal DNA circles, and abnormal nucleolar material – are sequestered away from chromosomes during meiosis II and subsequently eliminated. A similar sequestration and elimination process occurs for the core subunits of the nuclear pore complex in both young and old cells. Nuclear envelope remodeling drives the formation of a membranous compartment containing the sequestered material. Importantly,de novogeneration of plasma membrane is required for the sequestration event, preventing the inheritance of long-lived nucleoporins and senescence factors into the newly formed gametes. Our study uncovers a new mechanism of nuclear quality control and provides insight into its function in meiotic cellular rejuvenation.

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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