scholarly journals RNF135, RING finger protein, promotes the proliferation of human glioblastoma cells in vivo and in vitro via the ERK pathway

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Yongjian Liu ◽  
Feng Wang ◽  
Yongsheng Liu ◽  
Yiqun Yao ◽  
Xiupeng Lv ◽  
...  
Keyword(s):  
Ring Finger ◽  
Erk Pathway ◽  
Ring Finger Protein ◽  
Glioblastoma Cells ◽  
Human Glioblastoma ◽  
Finger Protein ◽  
Human Glioblastoma Cells

scholarly journals Ring Finger Protein 213 Assembles into a Sensor for ISGylated Proteins with Antimicrobial Activity

2021 ◽  
Author(s):  
Fabien Thery ◽  
Lia Martina ◽  
Caroline Asselman ◽  
Heidi Repo ◽  
Yifeng Zhang ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Ring Finger ◽  
Ring Finger Protein ◽  
Microbial Infection ◽  
Herpes Simplex Virus 1 ◽  
Finger Protein ◽  
Syncytial Virus ◽  
Simplex Virus

ISG15 is an interferon-stimulated, ubiquitin-like protein that can conjugate to substrate proteins (ISGylation) to counteract microbial infection, but the underlying mechanisms remain elusive. Here, we used a viral-like particle trapping technology to identify ISG15-binding proteins and discovered Ring Finger Protein 213 (RNF213) as an ISG15 interactor and cellular sensor of ISGylated proteins. RNF213 is a poorly-characterized, interferon-induced megaprotein that is frequently mutated in Moyamoya disease, a rare cerebrovascular disorder. We found that interferon induces ISGylation and oligomerization of RNF213 on lipid droplets, where it acts as a sensor for ISGylated proteins. We showed that RNF213 has broad antimicrobial activity in vitro and in vivo, counteracting infection with Listeria monocytogenes, herpes simplex virus 1 (HSV-1), human respiratory syncytial virus (RSV) and coxsackievirus B3 (CVB3), and we observed a striking co-localization of RNF213 with intracellular bacteria. Together, our findings provide novel molecular insights into the ISGylation pathway and reveal RNF213 as a key antimicrobial effector.

Down-regulation of ribosomal protein S15A inhibits proliferation of human glioblastoma cells in vivo and in vitro via AKT pathway

Tumor Biology ◽  
2015 ◽  
Vol 37 (4) ◽  
pp. 4979-4990 ◽  
Author(s):  
Yiqun Yao ◽  
Yongjian Liu ◽  
Xiupeng Lv ◽  
Bin Dong ◽  
Feng Wang ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Akt Pathway ◽  
Glioblastoma Cells ◽  
Down Regulation ◽  
Human Glioblastoma ◽  
Human Glioblastoma Cells

scholarly journals Ring finger protein 213 assembles into a sensor for ISGylated proteins with antimicrobial activity

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Fabien Thery ◽  
Lia Martina ◽  
Caroline Asselman ◽  
Yifeng Zhang ◽  
Madeleine Vessely ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Ring Finger ◽  
Ring Finger Protein ◽  
Microbial Infection ◽  
Herpes Simplex Virus 1 ◽  
Finger Protein ◽  
Syncytial Virus ◽  
Simplex Virus

AbstractISG15 is an interferon-stimulated, ubiquitin-like protein that can conjugate to substrate proteins (ISGylation) to counteract microbial infection, but the underlying mechanisms remain elusive. Here, we use a virus-like particle trapping technology to identify ISG15-binding proteins and discover Ring Finger Protein 213 (RNF213) as an ISG15 interactor and cellular sensor of ISGylated proteins. RNF213 is a poorly characterized, interferon-induced megaprotein that is frequently mutated in Moyamoya disease, a rare cerebrovascular disorder. We report that interferon induces ISGylation and oligomerization of RNF213 on lipid droplets, where it acts as a sensor for ISGylated proteins. We show that RNF213 has broad antimicrobial activity in vitro and in vivo, counteracting infection with Listeria monocytogenes, herpes simplex virus 1, human respiratory syncytial virus and coxsackievirus B3, and we observe a striking co-localization of RNF213 with intracellular bacteria. Together, our findings provide molecular insights into the ISGylation pathway and reveal RNF213 as a key antimicrobial effector.

scholarly journals Long-term In Vitro Treatment of Human Glioblastoma Cells with Temozolomide Increases Resistance In Vivo through Up-regulation of GLUT Transporter and Aldo-Keto Reductase Enzyme AKR1C Expression

Neoplasia ◽  
2010 ◽  
Vol 12 (9) ◽  
pp. 727-739 ◽  
Author(s):  
Benjamin Le Calvé ◽  
Michal Rynkowski ◽  
Marie Le Mercier ◽  
Céline Bruyère ◽  
Caroline Lonez ◽  
...  
Keyword(s):  
Glioblastoma Cells ◽  
Human Glioblastoma ◽  
Human Glioblastoma Cells ◽  
In Vitro Treatment

scholarly journals RNF5, a RING Finger Protein That Regulates Cell Motility by Targeting Paxillin Ubiquitination and Altered Localization

2003 ◽  
Vol 23 (15) ◽  
pp. 5331-5345 ◽  
Author(s):  
Christine Didier ◽  
Limor Broday ◽  
Anindita Bhoumik ◽  
Sharon Israeli ◽  
Shoichi Takahashi ◽  
...  
Keyword(s):  
Cell Motility ◽  
Ring Finger ◽  
Focal Adhesions ◽  
Normal Growth ◽  
Ring Finger Protein ◽  
C Elegans ◽  
Amino Terminal ◽  
Finger Protein

ABSTRACT RNF5 is a RING finger protein found to be important in the growth and development of Caenorhabditis elegans. The search for RNF5-associated proteins via a yeast two-hybrid screen identified a LIM-containing protein in C. elegans which shows homology with human paxillin. Here we demonstrate that the human homologue of RNF5 associates with the amino-terminal domain of paxillin, resulting in its ubiquitination. RNF5 requires intact RING and C-terminal domains to mediate paxillin ubiquitination. Whereas RNF5 mediates efficient ubiquitination of paxillin in vivo, protein extracts were required for in vitro ubiquitination, suggesting that additional modifications and/or an associated E3 ligase assist RNF5 targeting of paxillin ubiquitination. Mutant Ubc13 efficiently inhibits RNF5 ubiquitination, suggesting that RNF5 generates polychain ubiquitin of the K63 topology. Expression of RNF5 increases the cytoplasmic distribution of paxillin while decreasing its localization within focal adhesions, where it is primarily seen under normal growth. Concomitantly, RNF5 expression results in inhibition of cell motility. Via targeting of paxillin ubiquitination, which alters its localization, RNF5 emerges as a novel regulator of cell motility.

Expression and release of interleukin-1 by human glioblastoma cells in vitro and in vivo

1993 ◽  
Vol 121 (3-4) ◽  
pp. 199-205 ◽  
Author(s):  
T. Gauthier ◽  
M. -F. Hamou ◽  
L. Monod ◽  
P. Gallay ◽  
St. Carrel ◽  
...  
Keyword(s):  
Interleukin 1 ◽  
Glioblastoma Cells ◽  
Human Glioblastoma ◽  
Human Glioblastoma Cells

Production of interleukin-1 receptor antagonist by human glioblastoma cells in vitro and in vivo

1994 ◽  
Vol 50 (2) ◽  
pp. 187-194 ◽  
Author(s):  
Mitsuhiro Tada ◽  
Annie-Claire Diserens ◽  
Isabelle Desbaillets ◽  
Rehana Jaufeerally ◽  
Marie-France Hamou ◽  
...  
Keyword(s):  
Receptor Antagonist ◽  
Interleukin 1 ◽  
Glioblastoma Cells ◽  
Human Glioblastoma ◽  
Interleukin 1 Receptor Antagonist ◽  
Human Glioblastoma Cells
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