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Last update 08 May 2025

PARIS

Last update 08 May 2025

Basic Info

Synonyms

FLJ31413, PARIS, Parkin-interacting substrate

+ [2]

Introduction

Transcription repressor that specifically binds to the 5'-TATTTT[T/G]-3' consensus sequence on promoters and repress transcription of PGC-1-alpha (PPARGC1A), thereby playing a role in regulation of neuron death.

Drugs associated with PARIS

Farnesol

Target

PARIS

Mechanism

PARIS inhibitors

Active Org.

Samsung Biomedical Research Institute [+1]

Originator Org.

Samsung Biomedical Research Institute

Active Indication

Parkinson Disease [+1]

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Clinical Trials associated with PARIS

CTRI/2021/03/032330

/ Not yet recruitingPhase 2IIT

Antimicrobial efficiency of Farnesol as an intracanal medicament in patients with apical periodontitis - A Randomized Clinical Trial

Start Date29 Mar 2021

Sponsor / Collaborator-

100 Clinical Results associated with PARIS

100 Translational Medicine associated with PARIS

0 Patents (Medical) associated with PARIS

Literatures (Medical) associated with PARIS

01 Jun 2025·IBRO Neuroscience Reports

Genetic variants of ZNF746 and the level of plasma Parkin, PINK1, and ZNF746 proteins in patients with Parkinson's disease

Article

Author: Słowikowski, Bartosz ; Szymanowicz, Oliwia ; Owecki, Wojciech ; Goutor, Ulyana ; Dezor, Mateusz ; Dorszewska, Jolanta ; Kozubski, Wojciech ; Florczak-Wyspiańska, Jolanta ; Jagodziński, Paweł P

The occurrence of Parkinson's disease (PD) is influenced by a combination of genetic and environmental factors. Genetic variants of PARK2 (PRKN), PARK6 (PINK1), ZNF746, and their protein products are considered parameters related to the occurrence and development of PD. There is an interplay between Parkin, PINK1, and ZNF746 proteins. Inactivation of Parkin or PINK1 proteins results in elevated levels of the neurotoxic ZNF746 protein and loss of dopaminergic neurons. The objective of this study was to investigate the genetic variations in ZNF746 and the levels of Parkin, PINK1, and ZNF746 proteins in both PD patients and controls within the Polish population. The study included 125 controls and 100 PD patients. Genetic variants were analyzed using PCR-HRM and sequencing. The concentration of Parkin, PINK1, and ZNF746 proteins in plasma was determined by ELISA. The presence of three new genetic variants of ZNF746, chr7:149492883 G>A, ch7:149492890 G>A, ch7:149492694 G>A was demonstrated and the occurrence of ZNF746 c.473 G>A and ch7:149492754 A>G (rs191173107) was confirmed in Polish subjects. There was a significant decrease in Parkin concentration (p < 0.05) observed in PD patients when compared to controls. Reduced levels of Parkin were correlated with a significant rise in the concentration of ZNF746 (p < 0.05) in PD patients when compared with controls. PINK1 protein exhibited no notable alterations in concentration, except in patients who carried the heterozygous ZNF746 variant at ch7:149492694 G>A. The study of ZNF746 variants combined with the assessment of levels of Parkin, PINK1, and ZNF746 proteins provides fresh insights into our understanding of PD pathogenesis.

10 Oct 2024·Nature

Architecture and activation mechanism of the bacterial PARIS defence system

Article

Author: Liang, Qishan ; Enustun, Eray ; Deep, Amar ; Pogliano, Joe ; Corbett, Kevin D

Bacteria and their viruses (bacteriophages or phages) are engaged in an intense evolutionary arms race^1-5. While the mechanisms of many bacterial antiphage defence systems are known¹, how these systems avoid toxicity outside infection yet activate quickly after infection is less well understood. Here we show that the bacterial phage anti-restriction-induced system (PARIS) operates as a toxin-antitoxin system, in which the antitoxin AriA sequesters and inactivates the toxin AriB until triggered by the T7 phage counterdefence protein Ocr. Using cryo-electron microscopy, we show that AriA is related to SMC-family ATPases but assembles into a distinctive homohexameric complex through two oligomerization interfaces. In uninfected cells, the AriA hexamer binds to up to three monomers of AriB, maintaining them in an inactive state. After Ocr binding, the AriA hexamer undergoes a structural rearrangement, releasing AriB and allowing it to dimerize and activate. AriB is a toprim/OLD-family nuclease, the activation of which arrests cell growth and inhibits phage propagation by globally inhibiting protein translation through specific cleavage of a lysine tRNA. Collectively, our findings reveal the intricate molecular mechanisms of a bacterial defence system triggered by a phage counterdefence protein, and highlight how an SMC-family ATPase has been adapted as a bacterial infection sensor.

10 Oct 2024·Nature

A virally encoded tRNA neutralizes the PARIS antiviral defence system

Article

Author: Buyukyoruk, Murat ; Wiedenheft, Blake ; Wilkinson, Royce A ; Depardieu, Florence ; Belukhina, Svetlana ; Zahl, Trevor ; Chechenina, Anna ; Tesson, Florian ; Rouillon, Christophe ; Santiago-Frangos, Andrew ; Koszul, Romain ; Saudemont, Baptiste ; Hauryliuk, Vasili ; Isaev, Artem ; Morozova, Natalia ; Thierry, Agnès ; Shyrokova, Lena ; Skutel, Mikhail ; Bernheim, Aude ; Henriques, William S ; Burman, Nathaniel ; Livenskyi, Alexei ; Kurata, Tatsuaki ; Groseille, Justine ; Bikard, David ; Graham, Ava B ; Severinov, Konstantin

Viruses compete with each other for limited cellular resources, and some deliver defence mechanisms that protect the host from competing genetic parasites¹. The phage antirestriction induced system (PARIS) is a defence system, often encoded in viral genomes, that is composed of a 55 kDa ABC ATPase (AriA) and a 35 kDa TOPRIM nuclease (AriB)². However, the mechanism by which AriA and AriB function in phage defence is unknown. Here we show that AriA and AriB assemble into a 425 kDa supramolecular immune complex. We use cryo-electron microscopy to determine the structure of this complex, thereby explaining how six molecules of AriA assemble into a propeller-shaped scaffold that coordinates three subunits of AriB. ATP-dependent detection of foreign proteins triggers the release of AriB, which assembles into a homodimeric nuclease that blocks infection by cleaving host lysine transfer RNA. Phage T5 subverts PARIS immunity through expression of a lysine transfer RNA variant that is not cleaved by PARIS, thereby restoring viral infection. Collectively, these data explain how AriA functions as an ATP-dependent sensor that detects viral proteins and activates the AriB toxin. PARIS is one of an emerging set of immune systems that form macromolecular complexes for the recognition of foreign proteins, rather than foreign nucleic acids³.

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