RING finger protein 10 prevents neointimal hyperplasia by promoting apoptosis in vitro and in vivo

Life Sciences ◽  
2018 ◽  
Vol 208 ◽  
pp. 325-332 ◽  
Author(s):  
Guiquan Yu ◽  
Jing Chen ◽  
Siyu Li ◽  
Peng Pu ◽  
Wei Huang ◽  
...  
Keyword(s):  
Neointimal Hyperplasia ◽  
Ring Finger ◽  
Ring Finger Protein ◽  
Finger Protein

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.

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 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.

scholarly journals In vitro assembly of a functional human CDK7-cyclin H complex requires MAT1, a novel 36 kDa RING finger protein.

1995 ◽  
Vol 14 (22) ◽  
pp. 5608-5617 ◽  
Author(s):  
J. P. Tassan ◽  
M. Jaquenoud ◽  
A. M. Fry ◽  
S. Frutiger ◽  
G. J. Hughes ◽  
...  
Keyword(s):  
Ring Finger ◽  
Ring Finger Protein ◽  
Finger Protein ◽  
In Vitro Assembly

scholarly journals Two Potato Proteins, Including a Novel RING Finger Protein (HIP1), Interact with the Potyviral Multifunctional Protein HCpro

2003 ◽  
Vol 16 (5) ◽  
pp. 405-410 ◽  
Author(s):  
Deyin Guo ◽  
Carl Spetz ◽  
Mart Saarma ◽  
Jari P. T. Valkonen
Keyword(s):  
Ring Finger ◽  
Single Copy ◽  
Cellular Protein ◽  
Amino Acid Sequences ◽  
Ring Finger Protein ◽  
Potato Leaf ◽  
Multifunctional Protein ◽  
Potato Genome ◽  
Finger Protein

Potyviral helper-component proteinase (HCpro) is a multifunctional protein exerting its cellular functions in interaction with putative host proteins. In this study, cellular protein partners of the HCpro encoded by Potato virus A (PVA) (genus Potyvirus) were screened in a potato leaf cDNA library using a yeast two-hybrid system. Two cellular proteins were obtained that interact specifically with PVA HCpro in yeast and in the two in vitro binding assays used. Both proteins are encoded by single-copy genes in the potato genome. Analysis of the deduced amino acid sequences revealed that one (HIP1) of the two HCpro interactors is a novel RING finger protein. The sequence of the other protein (HIP2) showed no resemblance to the protein sequences available from databanks and has known biological functions.

scholarly journals Identification of a Novel RING Finger Protein as a Coregulator in Steroid Receptor-Mediated Gene Transcription

1998 ◽  
Vol 18 (9) ◽  
pp. 5128-5139 ◽  
Author(s):  
Anu-Maarit Moilanen ◽  
Hetti Poukka ◽  
Ulla Karvonen ◽  
Marika Häkli ◽  
Olli A. Jänne ◽  
...  
Keyword(s):  
Mammalian Cells ◽  
Ring Finger ◽  
Steroid Receptor ◽  
Rat Tissues ◽  
Physical Interaction ◽  
Ring Finger Protein ◽  
Basal Transcription ◽  
Cell Extracts ◽  
Finger Protein

ABSTRACT Using the DNA-binding domain of androgen receptor (AR) as a bait in a yeast two-hybrid screening, we have identified a small nuclear RING finger protein, termed SNURF, that interacts with AR in a hormone-dependent fashion in both yeast and mammalian cells. Physical interaction between AR and SNURF was demonstrated by coimmunoprecipitation from cell extracts and by protein-protein affinity chromatography. Rat SNURF is a highly hydrophilic protein consisting of 194 amino acid residues and comprising a consensus C3HC4 zinc finger (RING) structure in the C-terminal region and a bipartite nuclear localization signal near the N terminus. Immunohistochemical experiments indicated that SNURF is a nuclear protein. SNURF mRNA is expressed in a variety of human and rat tissues. Overexpression of SNURF in cultured mammalian cells enhanced not only androgen, glucocorticoid, and progesterone receptor-dependent transactivation but also basal transcription from steroid-regulated promoters. Mutation of two of the potential Zn2+coordinating cysteines to serines in the RING finger completely abolished the ability of SNURF to enhance basal transcription, whereas its ability to activate steroid receptor-dependent transcription was maintained, suggesting that there are separate domains in SNURF that mediate interactions with different regulatory factors. SNURF is capable of interacting in vitro with the TATA-binding protein, and the RING finger domain is needed for this interaction. Collectively, we have identified and characterized a ubiquitously expressed RING finger protein, SNURF, that may function as a bridging factor and regulate steroid receptor-dependent transcription by a mechanism different from those of previously identified coactivator or integrator proteins.

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