scholarly journals Cell cycle regulation of VCIP135 deubiquitinase activity and function in p97/p47-mediated Golgi reassembly

2015 ◽  
Vol 26 (12) ◽  
pp. 2242-2251 ◽  
Author(s):  
Xiaoyan Zhang ◽  
Yanzhuang Wang
Keyword(s):  
Cell Cycle ◽  
Membrane Fusion ◽  
Mammalian Cells ◽  
Membrane Dynamics ◽  
Deubiquitinating Enzyme ◽  
Golgi Membrane ◽  
Interacting Protein ◽  
Daughter Cells ◽  
And Function ◽  
Cycle Regulation

In mammalian cells, the inheritance of the Golgi apparatus into the daughter cells during each cycle of cell division is mediated by a disassembly and reassembly process, and this process is precisely controlled by phosphorylation and ubiquitination. VCIP135 (valosin-containing protein p97/p47 complex–interacting protein, p135), a deubiquitinating enzyme required for p97/p47-mediated postmitotic Golgi membrane fusion, is phosphorylated at multiple sites during mitosis. However, whether phosphorylation directly regulates VCIP135 deubiquitinase activity and Golgi membrane fusion in the cell cycle remains unknown. We show that, in early mitosis, phosphorylation of VCIP135 by Cdk1 at a single residue, S130, is sufficient to inactivate the enzyme and inhibit p97/p47-mediated Golgi membrane fusion. At the end of mitosis, VCIP135 S130 is dephosphorylated, which is accompanied by the recovery of its deubiquitinase activity and Golgi reassembly. Our results demonstrate that phosphorylation and ubiquitination are coordinated via VCIP135 to control Golgi membrane dynamics in the cell cycle.

scholarly journals Cell cycle regulation of Golgi membrane dynamics

2013 ◽  
Vol 23 (6) ◽  
pp. 296-304 ◽  
Author(s):  
Danming Tang ◽  
Yanzhuang Wang
Keyword(s):  
Cell Cycle ◽  
Cell Cycle Regulation ◽  
Membrane Dynamics ◽  
Golgi Membrane ◽  
Cycle Regulation

scholarly journals Ubiquitin and cell cycle regulation of Golgi membrane dynamics

2013 ◽  
Vol 27 (S1) ◽  
Author(s):  
Yanzhuang Wang ◽  
Danming Tang ◽  
Xiaoyan Zhang
Keyword(s):  
Cell Cycle ◽  
Cell Cycle Regulation ◽  
Membrane Dynamics ◽  
Golgi Membrane ◽  
Cycle Regulation

scholarly journals DjA1 maintains Golgi integrity via interaction with GRASP65

2019 ◽  
Vol 30 (4) ◽  
pp. 478-490 ◽  
Author(s):  
Jie Li ◽  
Danming Tang ◽  
Stephen C. Ireland ◽  
Yanzhuang Wang
Keyword(s):  
Heat Shock ◽  
Membrane Fusion ◽  
Structure Formation ◽  
Mammalian Cells ◽  
Binding Protein ◽  
Golgi Membrane ◽  
Biochemical Methods ◽  
Golgi Fragmentation ◽  
Golgi Structure

In mammalian cells, the Golgi reassembly stacking protein of 65 kDa (GRASP65) has been implicated in both Golgi stacking and ribbon linking by forming trans-oligomers. To better understand its function and regulation, we used biochemical methods to identify the DnaJ homolog subfamily A member 1 (DjA1) as a novel GRASP65-binding protein. In cells, depletion of DjA1 resulted in Golgi fragmentation, short and improperly aligned cisternae, and delayed Golgi reassembly after nocodazole washout. In vitro, immunodepletion of DjA1 from interphase cytosol reduced its activity to enhance GRASP65 oligomerization and Golgi membrane fusion, while adding purified DjA1 enhanced GRASP65 oligomerization. DjA1 is a cochaperone of Heat shock cognate 71-kDa protein (Hsc70), but the activity of DjA1 in Golgi structure formation is independent of its cochaperone activity or Hsc70, rather, through DjA1-GRASP65 interaction to promote GRASP65 oligomerization. Thus, DjA1 interacts with GRASP65 to enhance Golgi structure formation through the promotion of GRASP65 trans-oligomerization.

Calcium and cell cycle control

Development ◽  
1990 ◽  
Vol 108 (4) ◽  
pp. 525-542 ◽  
Author(s):  
M. Whitaker ◽  
R. Patel
Keyword(s):  
Cell Cycle ◽  
Sea Urchin ◽  
Mammalian Cells ◽  
Cell Cycle Regulation ◽  
Sea Urchins ◽  
Cell Cycle Control ◽  
Control Point ◽  
Control Cell ◽  
Free Calcium ◽  
Cycle Regulation

The cell division cycle of the early sea urchin embryo is basic. Nonetheless, it has control points in common with the yeast and mammalian cell cycles, at START, mitosis ENTRY and mitosis EXIT. Progression through each control point in sea urchins is triggered by transient increases in intracellular free calcium. The Cai transients control cell cycle progression by translational and post-translational regulation of the cell cycle control proteins pp34 and cyclin. The START Cai transient leads to phosphorylation of pp34 and cyclin synthesis. The mitosis ENTRY Cai transient triggers cyclin phosphorylation. The motosis EXIT transient causes destruction of phosphorylated cyclin. We compare cell cycle regulation by calcium in sea urchin embryos to cell cycle regulation in other eggs and oocytes and in mammalian cells.

scholarly journals Cilia and the cell cycle?

2005 ◽  
Vol 169 (5) ◽  
pp. 707-710 ◽  
Author(s):  
Lynne M. Quarmby ◽  
Jeremy D.K. Parker
Keyword(s):  
Cell Cycle ◽  
Kidney Disease ◽  
Polycystic Kidney Disease ◽  
Mammalian Cells ◽  
Cell Cycle Regulation ◽  
Polycystic Kidney ◽  
Unicellular Alga ◽  
Regulatory Relationship ◽  
Cycle Regulation ◽  
Multiple Signaling

A recent convergence of data indicating a relationship between cilia and proliferative diseases, such as polycystic kidney disease, has revived the long-standing enigma of the reciprocal regulatory relationship between cilia and the cell cycle. Multiple signaling pathways are localized to cilia in mammalian cells, and some proteins have been shown to act both in the cilium and in cell cycle regulation. Work from the unicellular alga Chlamydomonas is providing novel insights as to how cilia and the cell cycle are coordinately regulated.

scholarly journals Phosphorylation by Casein Kinase 2 Regulates Nap1 Localization and Function

2007 ◽  
Vol 28 (4) ◽  
pp. 1313-1325 ◽  
Author(s):  
Meredith E. K. Calvert ◽  
Kristin M. Keck ◽  
Celeste Ptak ◽  
Jeffrey Shabanowitz ◽  
Donald F. Hunt ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Casein Kinase ◽  
Casein Kinase 2 ◽  
S Phase ◽  
Bud Formation ◽  
Evolutionarily Conserved ◽  
Assembly Factor ◽  
And Function ◽  
Cycle Regulation

ABSTRACT In Saccharomyces cerevisiae, the evolutionarily conserved nucleocytoplasmic shuttling protein Nap1 is a cofactor for the import of histones H2A and H2B, a chromatin assembly factor and a mitotic factor involved in regulation of bud formation. To understand the mechanism by which Nap1 function is regulated, Nap1-interacting factors were isolated and identified by mass spectrometry. We identified several kinases among these proteins, including casein kinase 2 (CK2), and a new bud neck-associated protein, Nba1. Consistent with our identification of the Nap1-interacting kinases, we showed that Nap1 is phosphorylated in vivo at 11 sites and that Nap1 is phosphorylated by CK2 at three substrate serines. Phosphorylation of these serines was not necessary for normal bud formation, but mutation of these serines to either alanine or aspartic acid resulted in cell cycle changes, including a prolonged S phase, suggesting that reversible phosphorylation by CK2 is important for cell cycle regulation. Nap1 can shuttle between the nucleus and cytoplasm, and we also showed that CK2 phosphorylation promotes the import of Nap1 into the nucleus. In conclusion, our data show that Nap1 phosphorylation by CK2 appears to regulate Nap1 localization and is required for normal progression through S phase.

scholarly journals DREAM represses distinct targets by cooperating with different THAP domain proteins

2020 ◽  
Author(s):  
Csenge Gal ◽  
Francesco Nicola Carelli ◽  
Alex Appert ◽  
Chiara Cerrato ◽  
Ni Huang ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Mechanism Of Action ◽  
Cell Cycle Regulation ◽  
Gene Body ◽  
C Elegans ◽  
Cellular Quiescence ◽  
And Function ◽  
Cycle Regulation

ABSTRACTThe DREAM (DP, Retinoblastoma [Rb]-like, E2F, and MuvB) complex controls cellular quiescence by repressing cell cycle and other genes, but its mechanism of action is unclear. Here we demonstrate that two C. elegans THAP domain proteins, LIN-15B and LIN-36, co-localize with DREAM and function by different mechanisms for repression of distinct sets of targets. LIN-36 represses classical cell cycle targets by promoting DREAM binding and gene body enrichment of H2A.Z, and we find that DREAM subunit EFL-1/E2F is specific for LIN-36 targets. In contrast, LIN-15B represses germline specific targets in the soma by facilitating H3K9me2 promoter marking. We further find that LIN-36 and LIN-15B differently regulate DREAM binding. In humans, THAP proteins have been implicated in cell cycle regulation by poorly understood mechanisms. We propose that THAP domain proteins are key mediators of Rb/DREAM function.

scholarly journals 2P193 Cell cycle-dependent dynamics of the endoplasmic reticulum (ER) in mammalian cells (II) : Mechanism of membrane fusion of the ER

2004 ◽  
Vol 44 (supplement) ◽  
pp. S158
Author(s):  
F. Kano ◽  
H. Kondo ◽  
S. Yamauchi ◽  
A.R. Tanaka ◽  
N. Hosokawa ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Endoplasmic Reticulum ◽  
Membrane Fusion ◽  
Mammalian Cells ◽  
Cycle Dependent
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