scholarly journals Role of p97 AAA-ATPase in the Retrotranslocation of the Cholera Toxin A1 Chain, a Non-ubiquitinated Substrate

2005 ◽  
Vol 280 (30) ◽  
pp. 28127-28132 ◽  
Author(s):  
Michael Kothe ◽  
Yihong Ye ◽  
Jessica S. Wagner ◽  
Heidi E. De Luca ◽  
Eli Kern ◽  
...  
Keyword(s):  
Cholera Toxin ◽  
Aaa Atpase ◽  
Ubiquitinated Substrate

On the Role of Intramural Nerves in the Pathogenesis of Cholera Toxin-induced Intestinal Secretion

1981 ◽  
Vol 16 (3) ◽  
pp. 377-384 ◽  
Author(s):  
J. Cassuto ◽  
M. Jodal ◽  
R. Tuttle ◽  
O. Lundgren
Keyword(s):  
Cholera Toxin ◽  
Intestinal Secretion

Cellular Samurai: katanin and the severing of microtubules

2000 ◽  
Vol 113 (16) ◽  
pp. 2821-2827 ◽  
Author(s):  
L. Quarmby
Keyword(s):  
Epithelial Cells ◽  
Essential Role ◽  
Aaa Atpase ◽  
C Elegans ◽  
Microtubule Severing ◽  
Biochemical Studies ◽  
New Evidence

Recent biochemical studies of the AAA ATPase, katanin, provide a foundation for understanding how microtubules might be severed along their length. These in vitro studies are complemented by a series of recent reports of direct in vivo observation of microtubule breakage, which indicate that the in vitro phenomenon of catalysed microtubule severing is likely to be physiological. There is also new evidence that microtubule severing by katanin is important for the production of non-centrosomal microtubules in cells such as neurons and epithelial cells. Although it has been difficult to establish the role of katanin in mitosis, new genetic evidence indicates that a katanin-like protein, MEI-1, plays an essential role in meiosis in C. elegans. Finally, new proteins involved in the severing of axonemal microtubules have been discovered in the deflagellation system of Chlamydomonas.

scholarly journals The Role of the N-Domain in the ATPase Activity of the Mammalian AAA ATPase p97/VCP

2012 ◽  
Vol 287 (11) ◽  
pp. 8561-8570 ◽  
Author(s):  
Hajime Niwa ◽  
Caroline A. Ewens ◽  
Chun Tsang ◽  
Heidi O. Yeung ◽  
Xiaodong Zhang ◽  
...  
Keyword(s):  
Atpase Activity ◽  
Aaa Atpase

scholarly journals TRIP13 promotes the cell proliferation, migration and invasion of glioblastoma through the FBXW7/c-MYC axis

2019 ◽  
Vol 121 (12) ◽  
pp. 1069-1078 ◽  
Author(s):  
Guanghui Zhang ◽  
Qingzong Zhu ◽  
Gang Fu ◽  
Jianbing Hou ◽  
Xiaosong Hu ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
Therapeutic Target ◽  
Biological Effect ◽  
Thyroid Hormone Receptor ◽  
E3 Ubiquitin Ligase ◽  
Mitotic Checkpoint ◽  
Migration And Invasion ◽  
Cell Models ◽  
Aaa Atpase

Abstract Background Thyroid hormone receptor interactor 13 (TRIP13) is an AAA + ATPase that plays an important role in the mitotic checkpoint. TRIP13 is highly expressed in various human tumours and promotes tumorigenesis. However, the biological effect of TRIP13 in GBM cells remains unclear. Methods We generated GBM cell models with overexpressed or silenced TRIP13 via lentivirus-mediated overexpression and RNAi methods. The biological role of TRIP13 in the proliferation, migration and invasion of GBM cells has been further explored. Results Our research indicated that TRIP13 was highly expressed in GBM tissues and cells. We found that the proliferation, migration and invasion abilities were inhibited in TRIP13-knockdown GBM cells. These results indicated that TRIP13 plays an important role in the tumorigenesis of GBM. Moreover, we found that TRIP13 first stabilised c-MYC by inhibiting the transcription of FBXW7, which is an E3 ubiquitin ligase of c-MYC, by directly binding to the promoter region of FBXW7. Therefore, our study indicated that the TRIP13/FBXW7/c-MYC pathway might provide a prospective therapeutic target in the treatment of GBM. Conclusions These results indicated that TRIP13 plays an oncogenic role in GBM. The TRIP13/FBXW7/c-MYC pathway might act as a prospective therapeutic target for GBM patients.

STUDIES ON THE POSSIBLE ROLE OF CYCLIC AMP IN SOME ACTIONS OF CHOLERA TOXIN*

1971 ◽  
Vol 185 (1) ◽  
pp. 376-385 ◽  
Author(s):  
D. E. Schafer ◽  
W. D. Lust ◽  
J. B. Polson ◽  
J. Hedtke ◽  
B. Sircar ◽  
...  
Keyword(s):  
Cyclic Amp ◽  
Cholera Toxin

scholarly journals Attenuated Endocytosis and Toxicity of a Mutant Cholera Toxin with Decreased Ability To Cluster Ganglioside GM1 Molecules

2008 ◽  
Vol 76 (4) ◽  
pp. 1476-1484 ◽  
Author(s):  
Anne A. Wolf ◽  
Michael G. Jobling ◽  
David E. Saslowsky ◽  
Eli Kern ◽  
Kimberly R. Drake ◽  
...  
Keyword(s):  
Cholera Toxin ◽  
Host Cells ◽  
Wild Type ◽  
Intact Cells ◽  
B Subunit ◽  
Binding Pockets ◽  
Detergent Resistant Membranes ◽  
Toxin Uptake ◽  
Chimeric Toxins

ABSTRACT Cholera toxin (CT) moves from the plasma membrane (PM) of host cells to the endoplasmic reticulum (ER) by binding to the lipid raft ganglioside GM1. The homopentomeric B-subunit of the toxin can bind up to five GM1 molecules at once. Here, we examined the role of polyvalent binding of GM1 in CT action by producing chimeric CTs that had B-subunits with only one or two normal binding pockets for GM1. The chimeric toxins had attenuated affinity for binding to host cell PM, as expected. Nevertheless, like wild-type (wt) CT, the CT chimeras induced toxicity, fractionated with detergent-resistant membranes extracted from toxin-treated cells, displayed restricted diffusion in the plane of the PM in intact cells, and remained bound to GM1 when they were immunoprecipitated. Thus, binding normally to two or perhaps only one GM1 molecule is sufficient for association with lipid rafts in the PM and toxin action. The chimeric toxins, however, were much less potent than wt toxin, and they entered the cell by endocytosis more slowly, suggesting that clustering of GM1 molecules by the B-subunit enhances the efficiency of toxin uptake and perhaps also trafficking to the ER.

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