scholarly journals OPENER Is a Nuclear Envelope and Mitochondria Localized Protein Required for Cell Cycle Progression in Arabidopsis

2019 ◽  
Vol 31 (7) ◽  
pp. 1446-1465 ◽  
Author(s):  
Wei Wang ◽  
Xueyang Zhang ◽  
Totte Niittylä
PLoS Genetics ◽  
2012 ◽  
Vol 8 (11) ◽  
pp. e1003059 ◽  
Author(s):  
Sandra C. P. De Castro ◽  
Ashraf Malhas ◽  
Kit-Yi Leung ◽  
Peter Gustavsson ◽  
David J. Vaux ◽  
...  

2009 ◽  
Vol 122 (16) ◽  
pp. 2895-2905 ◽  
Author(s):  
M. D. McGee ◽  
I. Stagljar ◽  
D. A. Starr

2019 ◽  
Author(s):  
Arantxa Agote-Arán ◽  
Stephane Schmucker ◽  
Katerina Jerabkova ◽  
Inès Jmel Boyer ◽  
Alessandro Berto ◽  
...  

SummaryNucleoporins (Nups) build highly organized Nuclear Pore Complexes (NPCs) at the nuclear envelope (NE). Several Nups assemble into a sieve-like hydrogel within the central channel of the NPCs to regulate nucleocytoplasmic exchange. In the cytoplasm, a large excess of soluble Nups has been reported, but how their assembly is restricted to the NE is currently unknown. Here we show that Fragile X-related protein 1 (FXR1) can interact with several Nups and facilitate their localization to the NE during interphase through a microtubule and dynein-dependent mechanism. Downregulation of FXR1 or closely related orthologs FXR2 and Fragile X mental retardation protein (FMRP) leads to the accumulation of cytoplasmic Nup protein condensates. Likewise, several models of Fragile X syndrome (FXS), characterized by a loss of FMRP, also accumulate cytoplasmic Nup aggregates. These aggregate-containing cells display aberrant nuclear morphology and a delay in G1 cell cycle progression. Our results reveal an unexpected role for the FXR protein family and dynein in the spatial regulation of nucleoporin assembly.HighlightsCytoplasmic nucleoporins are assembled by Fragile X-related (FXR) proteins and dyneinFXR-Dynein pathway downregulation induces aberrant cytoplasmic aggregation of nucleoporinsCellular models of Fragile X syndrome accumulate aberrant cytoplasmic nucleoporin aggregates.FXR-Dynein pathway regulates nuclear morphology and G1 cell cycle progressioneTOC BlurbNucleoporins (Nups) form Nuclear Pore Complexes (NPCs) at the nuclear envelope. Agote-Arán at al. show how cells inhibit aberrant assembly of Nups in the cytoplasm and identify Fragile X-related (FXR) proteins and dynein that facilitate localization of Nups to the nuclear envelope and control G1 cell cycle progression.Graphical abstract


2014 ◽  
Vol 399 (1-2) ◽  
pp. 143-153 ◽  
Author(s):  
Mariana Santos ◽  
Patrícia Costa ◽  
Filipa Martins ◽  
Edgar F. da Cruz e Silva ◽  
Odete A. B. da Cruz e Silva ◽  
...  

2021 ◽  
Author(s):  
Viola Introini ◽  
Gururaj Rao Kidiyoor ◽  
Giancarlo Porcella ◽  
Marco Foiani ◽  
Pietro Cicuta ◽  
...  

The cell nucleus plays a central role in several key cellular processes, including chromosome organisation, replication and transcription. Recent work intriguingly suggests an association between nuclear mechanics and cell-cycle progression, but many aspects of this connection remain unexplored. Here, by monitoring nuclear shape fluctuations at different cell cycle stages, we uncover increasing inward fluctuations in late G2 and early mitosis, which are initially transient, but develop into instabilities that culminate into nuclear-envelope breakdown in mitosis. Perturbation experiments and correlation analysis reveal an association of these processes with chromatin condensation. We propose that the contrasting forces between an extensile stress and centripetal pulling from chromatin condensation could link mechanically chromosome condensation and nuclear-envelope breakdown, the two main nuclear processes during mitosis.


2011 ◽  
Vol 39 (6) ◽  
pp. 1742-1746 ◽  
Author(s):  
Vlastimil Srsen ◽  
Nadia Korfali ◽  
Eric C. Schirmer

The nuclear envelope is a complex double membrane system that serves as a dynamic interface between the nuclear and cytoplasmic compartments. Among its many roles is to provide an anchor for gene regulatory proteins on its nucleoplasmic surface and for the cytoskeleton on its cytoplasmic surface. Both sets of anchors are proteins called NETs (nuclear envelope transmembrane proteins), embedded respectively in the inner or outer nuclear membranes. Several lines of evidence indicate that the nuclear envelope contributes to cell-cycle regulation. These contributions come from both inner and outer nuclear membrane NETs and appear to operate through several distinct mechanisms ranging from sequestration of gene-regulatory proteins to activating kinase cascades.


EMBO Reports ◽  
2019 ◽  
Vol 20 (9) ◽  
Author(s):  
Julien Aureille ◽  
Valentin Buffière‐Ribot ◽  
Ben E Harvey ◽  
Cyril Boyault ◽  
Lydia Pernet ◽  
...  

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