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 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 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.

scholarly journals Mek and Cdc2 Kinase Are Sequentially Required for Golgi Disassembly in Mdck Cells by the Mitotic Xenopus Extracts

2000 ◽  
Vol 149 (2) ◽  
pp. 357-368 ◽  
Author(s):  
Fumi Kano ◽  
Katsuya Takenaka ◽  
Akitsugu Yamamoto ◽  
Kuniaki Nagayama ◽  
Eisuke Nishida ◽  
...  
Keyword(s):  
Golgi Apparatus ◽  
Molecular Mechanisms ◽  
Mdck Cells ◽  
Morphological Changes ◽  
Green Fluorescence Protein ◽  
Membrane Dynamics ◽  
Mitogen Activated Protein Kinase ◽  
Golgi Membrane ◽  
Cdc2 Kinase ◽  
Electron Microscopies

At the onset of mitosis, the Golgi apparatus, which consists of several cisternae, disperses throughout the cell to be partitioned into daughter cells. The molecular mechanisms of this process are now beginning to be understood. To investigate the biochemical requirements and kinetics of mitotic Golgi membrane dynamics in polarized cells, we have reconstituted the disassembly of the Golgi apparatus by introducing Xenopus egg extracts into permeabilized Mardin-Darby canine kidney (MDCK) cells. We used green fluorescence protein (GFP)-tagged galactosyltransferase-expressing MDCK cells to analyze the morphological changes of the Golgi membrane in the semi-intact system. Analyses by fluorescence and electron microscopies showed that the Golgi disassembly can be dissected into two elementary processes morphologically. In the first process, the perinuclear Golgi stacks break into punctate structures, intermediates, which are comprised of mini-stacks of cisternae associating with apical microtubule networks. In the second process, the structures fragment more thoroughly or substantially relocate to the ER. Our analyses further showed that cdc2 kinase and mitogen-activated protein kinase kinase (MAPKK = MEK) are differently involved in these two processes: the first process is mainly regulated by MEK and the second mainly by cdc2.

scholarly journals Expression of Golgi Membrane Protein p138 is Cell Cycle-independent and Dissociated from Centrosome Duplication

2002 ◽  
Vol 27 (2) ◽  
pp. 117-117 ◽  
Author(s):  
Kohei Doi ◽  
Shohei Noma ◽  
Fumiaki Yamao ◽  
Hideki Goko ◽  
Tatsuo Yagura
Keyword(s):  
Cell Cycle ◽  
Membrane Protein ◽  
Centrosome Duplication ◽  
Golgi Membrane

scholarly journals Brefeldin A-dependent Membrane Tubule Formation Reconstituted In Vitro Is Driven by a Cell Cycle–regulated Microtubule Motor

2000 ◽  
Vol 11 (3) ◽  
pp. 941-955 ◽  
Author(s):  
Alasdair M. Robertson ◽  
Victoria J. Allan
Keyword(s):  
Cell Cycle ◽  
Cultured Cells ◽  
Brefeldin A ◽  
Binding Activity ◽  
Membrane Dynamics ◽  
Dependent Manner ◽  
Tubule Formation ◽  
Early Endosomes

Treatment of cultured cells with brefeldin A (BFA) induces the formation of extensive membrane tubules from the Golgi apparatus,trans-Golgi network, and early endosomes in a microtubule-dependent manner. We have reconstituted this transport process in vitro using Xenopus egg cytosol and a rat liver Golgi-enriched membrane fraction. The presence of BFA results in the formation of an intricate, interconnected tubular membrane network, a process that, as in vivo, is inhibited by nocodazole, the H1 anti-kinesin monoclonal antibody, and by membrane pretreatment with guanosine 5′-O-(3-thiotriphosphate). Surprisingly, membrane tubule formation is not due to the action of conventional kinesin or any of the other motors implicated in Golgi membrane dynamics. Two candidate motors of ∼100 and ∼130 kDa have been identified using the H1 antibody, both of which exhibit motor properties in a biochemical assay. Finally, BFA-induced membrane tubule formation does not occur in metaphase cytosol, and because membrane binding of both candidate motors is not altered after incubation in metaphase compared with interphase cytosol, these results suggest that either the ATPase or microtubule-binding activity of the relevant motor is cell cycle regulated.

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