Cell Cycle-Dependent Phosphorylation of Nucleoporins and Nuclear Pore Membrane Protein Gp210†

Biochemistry ◽  
1996 ◽  
Vol 35 (24) ◽  
pp. 8035-8044 ◽  
Author(s):  
Catherine Favreau ◽  
Howard J. Worman ◽  
Richard W. Wozniak ◽  
Thierry Frappier ◽  
Jean-Claude Courvalin
Keyword(s):  
Cell Cycle ◽  
Membrane Protein ◽  
Nuclear Pore ◽  
Cycle Dependent

scholarly journals Cell Cycle-Dependent Differences in Nuclear Pore Complex Assembly in Metazoa

Cell ◽  
2010 ◽  
Vol 141 (6) ◽  
pp. 1030-1041 ◽  
Author(s):  
Christine M. Doucet ◽  
Jessica A. Talamas ◽  
Martin W. Hetzer
Keyword(s):  
Cell Cycle ◽  
Nuclear Pore Complex ◽  
Nuclear Pore ◽  
Complex Assembly ◽  
Cycle Dependent

scholarly journals Fragile X–Related Protein 1 Regulates Nucleoporin Localization in a Cell Cycle–Dependent Manner

2021 ◽  
Vol 9 ◽  
Author(s):  
Arantxa Agote-Arán ◽  
Junyan Lin ◽  
Izabela Sumara
Keyword(s):  
Cell Cycle ◽  
Mammalian Cells ◽  
Cell Cycle Progression ◽  
Fragile X ◽  
Protein Translation ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Dependent Manner ◽  
Independent Manner ◽  
Cycle Dependent

Nuclear pore complexes (NPCs) are embedded in the nuclear envelope (NE) where they ensure the transport of macromolecules between the nucleus and the cytoplasm. NPCs are built from nucleoporins (Nups) through a sequential assembly order taking place at two different stages during the cell cycle of mammalian cells: at the end of mitosis and during interphase. In addition, fragile X–related proteins (FXRPs) can interact with several cytoplasmic Nups and facilitate their localization to the NE during interphase likely through a microtubule-dependent mechanism. In the absence of FXRPs or microtubule-based transport, Nups aberrantly localize to the cytoplasm forming the so-called cytoplasmic nucleoporin granules (CNGs), compromising NPCs’ function on protein export. However, it remains unknown if Nup synthesis or degradation mechanisms are linked to the FXRP–Nup pathway and if and how the action of FXRPs on Nups is coordinated with the cell cycle progression. Here, we show that Nup localization defects observed in the absence of FXR1 are independent of active protein translation. CNGs are cleared in an autophagy- and proteasome-independent manner, and their presence is restricted to the early G1 phase of the cell cycle. Our results thus suggest that a pool of cytoplasmic Nups exists that contributes to the NPC assembly specifically during early G1 to ensure NPC homeostasis at a short transition from mitosis to the onset of interphase.

scholarly journals The ER morphology-regulating lunapark protein induces the formation of stacked bilayer discs

2018 ◽  
Vol 1 (1) ◽  
pp. e201700014 ◽  
Author(s):  
Songyu Wang ◽  
Robert E Powers ◽  
Vicki AM Gold ◽  
Tom A Rapoport
Keyword(s):  
Cell Cycle ◽  
Membrane Protein ◽  
Dependent Manner ◽  
Cytosolic Domains ◽  
A Cell ◽  
Constant Distance ◽  
Higher Eukaryotes ◽  
Cycle Dependent

Lunapark (Lnp) is a conserved membrane protein that localizes to and stabilizes three-way junctions of the tubular ER network. In higher eukaryotes, phosphorylation of Lnp may contribute to the conversion of the ER from tubules to sheets during mitosis. Here, we report on the reconstitution of purified Lnp with phospholipids. Surprisingly, Lnp induces the formation of stacked membrane discs. Each disc is a bicelle, with Lnp sitting in the bilayer facing both directions. The interaction between bicelles is mediated by the cytosolic domains of Lnp, resulting in a constant distance between the discs. A phosphomimetic Lnp mutant shows reduced bicelle stacking. Based on these results, we propose that Lnp tethers ER membranes in vivo in a cell cycle–dependent manner. Lnp appears to be the first membrane protein that induces the formation of stacked bicelles.

scholarly journals Cell-cycle-dependent phosphorylation of the nuclear pore Nup107-160 subcomplex

2007 ◽  
Vol 104 (10) ◽  
pp. 3811-3816 ◽  
Author(s):  
J. S. Glavy ◽  
A. N. Krutchinsky ◽  
I. M. Cristea ◽  
I. C. Berke ◽  
T. Boehmer ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Nuclear Pore ◽  
Cycle Dependent

Cell cycle dependent localization of the telomeric PARP, tankyrase, to nuclear pore complexes and centrosomes

1999 ◽  
Vol 112 (21) ◽  
pp. 3649-3656 ◽  
Author(s):  
S. Smith ◽  
T. de Lange
Keyword(s):  
Cell Cycle ◽  
Subcellular Fractionation ◽  
Negative Regulator ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Dependent Manner ◽  
Telomeric Dna ◽  
Cycle Dependent ◽  
Pore Complexes

Tankyrase is a human poly(ADP-ribose) polymerase that was initially identified through its interaction with the telomeric protein TRF1, a negative regulator of telomere length. In vitro poly(ADP-ribosyl)ation by tankyrase inhibits TRF1 binding to telomeric DNA suggesting a role for tankyrase in telomere function. We previously demonstrated that tankyrase co-localizes with TRF1 at the ends of human chromosomes in metaphase. Here we show that tankyrase localizes to additional subcellular sites in a cell cycle dependent manner. In interphase, tankyrase co-localized with TRF1 to telomeres, but in addition was found to reside at nuclear pore complexes, as evidenced by indirect immunofluorescence, subcellular fractionation and immunoelectron microscopy. At mitosis, concomitant with nuclear envelope breakdown and nuclear pore complex disassembly, tankyrase was found to relocate around the pericentriolar matrix of mitotic centrosomes. This complex staining pattern along with the observation that tankyrase did not contain a nuclear localization signal suggested that its telomeric localization might be regulated, perhaps by TRF1. Indeed, localization of exogenously-expressed tankyrase to telomeres was dependent upon co-transfection with TRF1. These data indicate that the subcellular localization of tankyrase can be regulated by both the cell cycle and TRF1.

Cell cycle dependent modulation of insulin and IGF I receptor binding to human Burkitt type ALL cells

1987 ◽  
Vol 116 (3_Suppl) ◽  
pp. S81
Author(s):  
U. VETTER ◽  
W. HARTMANN ◽  
H. HITZLER ◽  
W. HEIT ◽  
J. SCHLICKENRIEDER ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Receptor Binding ◽  
Igf I ◽  
Cycle Dependent
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