scholarly journals Phosphorylation regulates VCIP135 function in Golgi membrane fusion during the cell cycle

2013 ◽  
Vol 127 (1) ◽  
pp. 172-181 ◽  
Author(s):  
X. Zhang ◽  
H. Zhang ◽  
Y. Wang
Keyword(s):  
Cell Cycle ◽  
Membrane Fusion ◽  
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 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.

An NSF function distinct from ATPase-dependent SNARE disassembly is essential for Golgi membrane fusion

10.1038/14025 ◽  
1999 ◽  
Vol 1 (6) ◽  
pp. 335-340 ◽  
Author(s):  
Joyce M. M. Müller ◽  
Catherine Rabouille ◽  
Richard Newman ◽  
James Shorter ◽  
Paul Freemont ◽  
...  
Keyword(s):  
Membrane Fusion ◽  
Golgi Membrane

scholarly journals Sequential SNARE disassembly and GATE-16–GOS-28 complex assembly mediated by distinct NSF activities drives Golgi membrane fusion

2002 ◽  
Vol 157 (7) ◽  
pp. 1161-1173 ◽  
Author(s):  
Joyce M.M. Müller ◽  
James Shorter ◽  
Richard Newman ◽  
Katrin Deinhardt ◽  
Yuval Sagiv ◽  
...  
Keyword(s):  
Membrane Fusion ◽  
Atp Hydrolysis ◽  
Golgi Membrane ◽  
Complex Assembly ◽  
Evolutionarily Conserved ◽  
Golgi Fragmentation ◽  
Fusion Analysis

Characterization of mammalian NSF (G274E) and Drosophila NSF (comatose) mutants revealed an evolutionarily conserved NSF activity distinct from ATPase-dependent SNARE disassembly that was essential for Golgi membrane fusion. Analysis of mammalian NSF function during cell-free assembly of Golgi cisternae from mitotic Golgi fragments revealed that NSF disassembles Golgi SNAREs during mitotic Golgi fragmentation. A subsequent ATPase-independent NSF activity restricted to the reassembly phase is essential for membrane fusion. NSF/α-SNAP catalyze the binding of GATE-16 to GOS-28, a Golgi v-SNARE, in a manner that requires ATP but not ATP hydrolysis. GATE-16 is essential for NSF-driven Golgi reassembly and precludes GOS-28 from binding to its cognate t-SNARE, syntaxin-5. We suggest that this occurs at the inception of Golgi reassembly to protect the v-SNARE and regulate SNARE function.

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 Activation of myosin V–based motility and F-actin–dependent network formation of endoplasmic reticulum during mitosis

2002 ◽  
Vol 159 (4) ◽  
pp. 571-577 ◽  
Author(s):  
Torsten Wöllert ◽  
Dieter G. Weiss ◽  
Hans-Hermann Gerdes ◽  
Sergei A. Kuznetsov
Keyword(s):  
Cell Cycle ◽  
Endoplasmic Reticulum ◽  
Membrane Fusion ◽  
Network Formation ◽  
Active Role ◽  
Myosin V ◽  
Egg Extracts ◽  
Xenopus Egg ◽  
Xenopus Egg Extracts

It is widely believed that microtubule- and F-actin–based transport of cytoplasmic organelles and membrane fusion is down-regulated during mitosis. Here we show that during the transition of Xenopus egg extracts from interphase to metaphase myosin V–driven movement of small globular vesicles along F-actin is strongly inhibited. In contrast, the movement of ER and ER network formation on F-actin is up-regulated in metaphase extracts. Our data demonstrate that myosin V–driven motility of distinct organelles is differently controlled during the cell cycle and suggest an active role of F-actin in partitioning, positioning, and membrane fusion of the ER during cell division.

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

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

Mitotic phosphorylation of VCIP135 blocks p97ATPase-mediated Golgi membrane fusion

2013 ◽  
Vol 433 (2) ◽  
pp. 237-242 ◽  
Author(s):  
Go Totsukawa ◽  
Ayaka Matsuo ◽  
Ayano Kubota ◽  
Yuya Taguchi ◽  
Hisao Kondo
Keyword(s):  
Membrane Fusion ◽  
Golgi Membrane ◽  
Mitotic Phosphorylation
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