scholarly journals The ubiquitin ligase HACE1 regulates Golgi membrane dynamics during the cell cycle

2011 ◽  
Vol 2 (1) ◽  
Author(s):  
Danming Tang ◽  
Yi Xiang ◽  
Stefano De Renzis ◽  
Jochen Rink ◽  
Gen Zheng ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Ubiquitin Ligase ◽  
Membrane Dynamics ◽  
Golgi Membrane

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 Monoubiquitination Regulates Golgi Membrane Dynamics In The Cell Cycle

2015 ◽  
Vol 29 (S1) ◽  
Author(s):  
Yanzhuang Wang ◽  
Xiaoyan Zhang ◽  
Shijiao Huang
Keyword(s):  
Cell Cycle ◽  
Membrane Dynamics ◽  
Golgi Membrane

scholarly journals Monoubiquitination of Syntaxin 5 Regulates Golgi Membrane Dynamics during the Cell Cycle

2016 ◽  
Vol 38 (1) ◽  
pp. 73-85 ◽  
Author(s):  
Shijiao Huang ◽  
Danming Tang ◽  
Yanzhuang Wang
Keyword(s):  
Cell Cycle ◽  
Membrane Dynamics ◽  
Golgi Membrane

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 A Novel Golgi Membrane Protein Is a Partner of the ARF Exchange Factors Gea1p and Gea2p

2003 ◽  
Vol 14 (6) ◽  
pp. 2357-2371 ◽  
Author(s):  
Sophie Chantalat ◽  
Rëgis Courbeyrette ◽  
Francesca Senic-Matuglia ◽  
Catherine L. Jackson ◽  
Bruno Goud ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Protein Trafficking ◽  
Transmembrane Domain ◽  
Integral Membrane Protein ◽  
Membrane Dynamics ◽  
General Interest ◽  
Single Mutation ◽  
Golgi Membrane ◽  
Nucleotide Exchange

The Sec7 domain guanine nucleotide exchange factors (GEFs) for the GTPase ARF are highly conserved regulators of membrane dynamics and protein trafficking. The interactions of large ARF GEFs with cellular membranes for localization and/or activation are likely to participate in regulated recruitment of ARF and effectors. However, these interactions remain largely unknown. Here we characterize Gmh1p, the first Golgi transmembrane-domain partner of any of the high-molecular-weight ARF-GEFs. Gmh1p is an evolutionarily conserved protein. We demonstrate molecular interaction between the yeast Gmh1p and the large ARF-GEFs Gea1p and Gea2p. This interaction involves a domain of Gea1p and Gea2p that is conserved in the eukaryotic orthologues of the Gea proteins. A single mutation in a conserved amino acid residue of this domain is sufficient to abrogate the interaction, whereas the overexpression of Gmh1p can compensate in vivo defects caused by mutations in this domain. We show that Gmh1p is an integral membrane protein that localizes to the early Golgi in yeast and in human HeLa cells and cycles through the ER. Hence, we propose that Gmh1p acts as a positive Golgi-membrane partner for Gea function. These results are of general interest given the evolutionary conservation of both ARF-GEFs and the Gmh proteins.

Regulation of the cell cycle inhibitor p27 and its ubiquitin ligase Skp2 in differentiation of human embryonic stem cells

2007 ◽  
Vol 21 (11) ◽  
pp. 2807-2817 ◽  
Author(s):  
Dana Egozi ◽  
Maanit Shapira ◽  
Galit Paor ◽  
Ofer Ben‐Izhak ◽  
Karl Skorecki ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Stem Cells ◽  
Embryonic Stem Cells ◽  
Ubiquitin Ligase ◽  
Human Embryonic Stem Cells ◽  
Embryonic Stem ◽  
Cell Cycle Inhibitor

scholarly journals Hect E3 ubiquitin ligase Tom1 controls Dia2 degradation during the cell cycle

2012 ◽  
Vol 23 (21) ◽  
pp. 4203-4211 ◽  
Author(s):  
Dong-Hwan Kim ◽  
Deanna M. Koepp
Keyword(s):  
Cell Cycle ◽  
Protein Degradation ◽  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
S Phase ◽  
Temperature Sensitive ◽  
Dependent Manner ◽  
Charged Residues ◽  
Phase Progression ◽  
Positively Charged

The ubiquitin proteasome system plays a pivotal role in controlling the cell cycle. The budding yeast F-box protein Dia2 is required for genomic stability and is targeted for ubiquitin-dependent degradation in a cell cycle–dependent manner, but the identity of the ubiquitination pathway is unknown. We demonstrate that the Hect domain E3 ubiquitin ligase Tom1 is required for Dia2 protein degradation. Deletion of DIA2 partially suppresses the temperature-sensitive phenotype of tom1 mutants. Tom1 is required for Dia2 ubiquitination and degradation during G1 and G2/M phases of the cell cycle, whereas the Dia2 protein is stabilized during S phase. We find that Tom1 binding to Dia2 is enhanced in G1 and reduced in S phase, suggesting a mechanism for this proteolytic switch. Tom1 recognizes specific, positively charged residues in a Dia2 degradation/NLS domain. Loss of these residues blocks Tom1-mediated turnover of Dia2 and causes a delay in G1–to–S phase progression. Deletion of DIA2 rescues a delay in the G1–to–S phase transition in the tom1Δ mutant. Together our results suggest that Tom1 targets Dia2 for degradation during the cell cycle by recognizing positively charged residues in the Dia2 degradation/NLS domain and that Dia2 protein degradation contributes to G1–to–S phase progression.

scholarly journals The E3 ubiquitin ligase skp2 regulates neural differentiation independent from the cell cycle

2007 ◽  
Vol 2 (1) ◽  
pp. 27 ◽  
Author(s):  
Hector Boix-Perales ◽  
Ian Horan ◽  
Helen Wise ◽  
Horng-Ru Lin ◽  
Li-Chiou Chuang ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Ubiquitin Ligase ◽  
Neural Differentiation ◽  
E3 Ubiquitin Ligase

scholarly journals The role of SCF ubiquitin-ligase complex at the beginning of life

2019 ◽  
Vol 17 (1) ◽  
Author(s):  
Jiayan Xie ◽  
Yimei Jin ◽  
Guang Wang
Keyword(s):  
Cell Cycle ◽  
Ubiquitin Ligase ◽  
Cellular Proteins ◽  
Cell Cycle Regulators ◽  
Signal Transducers ◽  
E3 Ligases ◽  
Cellular Processes ◽  
Ubiquitin Ligase Complex ◽  
Scf Ubiquitin Ligase

AbstractAs the largest family of E3 ligases, the Skp1-cullin 1-F-box (SCF) E3 ligase complex is comprised of Cullins, Skp1 and F-box proteins. And the SCF E3 ubiquitin ligases play an important role in regulating critical cellular processes, which promote degradation of many cellular proteins, including signal transducers, cell cycle regulators, and transcription factors. We review the biological roles of the SCF ubiquitin-ligase complex in gametogenesis, oocyte-to-embryo transition, embryo development and the regulation for estrogen and progestin. We find that researches about the SCF ubiquitin-ligase complex at the beginning of life are not comprehensive, thus more in-depth researches will promote its eventual clinical application.

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