Article
Biology
C. Maresca, A. Dello Stritto, C. D'Angelo, E. Petti, A. Rizzo, E. Vertecchi, F. Berardinelli, L. Bonanni, A. Sgura, A. Antoccia, G. Graziani, A. Biroccio, E. Salvati
Summary: PARP1 interacts with TRF1 and modifies its DNA affinity, influencing telomere replication and helicase recruitment. This study uncovers a new role for PARP1 as a surveillant of telomere replication, orchestrating protein dynamics at the replication fork.
COMMUNICATIONS BIOLOGY
(2023)
Article
Biochemistry & Molecular Biology
Elise Rouleau-Turcotte, Dragomir B. Krastev, Stephen J. Pettitt, Christopher J. Lord, John M. Pascal
Summary: PARP1 can rapidly detect DNA strand break damage and activate the production of poly(ADP-ribose) by signaling break detection to its catalytic domain. This study provides insights into the contributions of the regulatory helical domain (HD) to PARP1 allostery and the interaction with DNA damage, as well as the mechanisms of PARP1 catalytic activation and retention on DNA damage.
Article
Pharmacology & Pharmacy
Zhenzhen Li, Zhen Guo, Rui Lan, Sidong Cai, Zhirong Lin, Jingyan Li, Junjian Wang, Zhuoming Li, Peiqing Liu
Summary: BRD4 is crucial in the pathogenesis of cardiac hypertrophy by interacting with PARP1 to induce hypertrophic gene expression and transcription activation. Targeting the inhibition of PARP1-BRD4 interactions may have therapeutic potential for pathological cardiac hypertrophy.
ACTA PHARMACEUTICA SINICA B
(2021)
Article
Cell Biology
Konstantin N. Naumenko, Mariya V. Sukhanova, Loic Hamon, Tatyana A. Kurgina, Rashid O. Anarbaev, Aswin Mangerich, David Pastre, Olga I. Lavrik
Summary: Y-box-binding protein 1 (YB-1) is involved in the regulation of gene expression and has been found to play a role in the regulation of PARP1 activity. The C-terminal domain of YB-1 is able to interact with PAR and control its synthesis, providing important insights into the regulation of PARP1 activity.
FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY
(2022)
Article
Biochemistry & Molecular Biology
Masato Mashimo, Momoko Kita, Arina Uno, Moe Nii, Moe Ishihara, Takuya Honda, Yuka Gotoh-Kinoshita, Atsuo Nomura, Hiroyuki Nakamura, Toshihiko Murayama, Ryoichi Kizu, Takeshi Fujii
Summary: Poly(ADP-ribosyl)ation is a post-translational modification process that transfers poly(ADP-ribose) to proteins. TNKS1/2 have been found to play important roles in neuronal development, promoting neurite outgrowth and synapse formation.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2022)
Article
Biochemistry & Molecular Biology
Bin Peng, Ruifeng Shi, Jing Bian, Yuwei Li, Peipei Wang, Hailong Wang, Ji Liao, Wei-Guo Zhu, Xingzhi Xu
Summary: PLK1 is enriched at DSBs in response to DNA damage, but dispersed by PARG. PAR chains directly bind to PLK1 and inhibit its enzymatic activity, while CHK1-mediated phosphorylation affects PLK1 activity towards RAD51, ultimately promoting HR repair.
NUCLEIC ACIDS RESEARCH
(2021)
Article
Multidisciplinary Sciences
Jyothi Mahadevan, Asmita Jha, Johannes Rudolph, Samuel Bowerman, Domenic Narducci, Anders S. Hansen, Karolin Luger
Summary: PARP1 contributes to genome architecture and DNA damage repair through its dynamic association with chromatin. PARP1/2 recognize damaged DNA and recruit the DNA repair machinery. Single-molecule microscopy in live cells revealed two classes of freely diffusing PARP1/2 and two classes of bound PARP1/2. Majority of PARP1/2 diffuse freely in both undamaged and damaged nuclei, while a small fraction becomes transiently bound upon laser-induced DNA damage. Treatment with PARP1/2 inhibitors in the presence of DNA damage causes subtle changes in the dynamics of bound PARP1/2, suggesting potential for targeted therapy.
Article
Medicine, Research & Experimental
Jeffrey Wang, Mohamed A. Ghonim, Salome Ibba, Hanh H. Luu, Yucel Aydin, Peter A. Greer, A. Hamid Boulares
Summary: This study reveals that poly(ADP-ribosyl)ation plays a critical role in protecting STAT6 from degradation, and can be synthetically targeted for degradation by inhibiting PARP-1. Additionally, the study identifies STAT6 as a bonafide substrate for chaperone-mediated autophagy in the human Jurkat cell-line.
JOURNAL OF TRANSLATIONAL MEDICINE
(2022)
Review
Oncology
Giulia Pinton, Sara Boumya, Maria Rosa Ciriolo, Fabio Ciccarone
Summary: This review article explores the role of PARP-1 and poly(ADP-ribosyl)ation in gene expression, DNA repair pathways, and genomic stability, including their impact on chromatin remodelling. The article specifically focuses on how PARP-1 directly modifies histone proteins and enzymes involved in DNA/histone epigenetic modifications to shape chromatin structure during transcription and DNA damage response. Understanding the role of poly(ADP-ribosyl)ation in regulating chromatin organization could provide insights into resistance mechanisms to PARP inhibitors and the clinical relevance of combining epigenetic drugs.
Review
Cell Biology
Palmiro Poltronieri, Angela Celetti, Luca Palazzo
Summary: NAD(+) is crucial in post-translational modification of proteins and nucleic acids, with its synthesis, degradation, and transport playing a vital role in maintaining optimal NAD(+) levels. The functional connection between NAD(+-utilizing enzymes and mono(ADP-ribosyl)ating enzymes is linked to chronic diseases.
Article
Biochemistry & Molecular Biology
Liang Kong, Baomin Feng, Yan Yan, Chao Zhang, Jun Hyeok Kim, Lahong Xu, Johannes Gregor Matthias Rack, Ying Wang, Jyan-Chyun Jang, Ivan Ahel, Libo Shan, Ping He
Summary: This study reveals that the noncanonical ADP-ribosyltransferase SRO2 mediates the MARylation of zinc finger proteins SZF1 and SZF2, key regulators of immune gene expression. MARylation antagonizes polyubiquitination of SZF1, stabilizing the protein and maintaining protein homeostasis to mediate immune responses.
Article
Biochemistry & Molecular Biology
T. A. Kurgina, O. I. Lavrik
Summary: Poly(ADP-ribose) (PAR) is a negatively charged polymer composed of ADP-ribose monomers that is synthesized by poly(ADP-ribose)polymerase (PARP) enzymes upon DNA damage. PARP1 and PARP2 are the most well-studied members of the PARP family and play crucial roles in regulating DNA repair. A newly discovered histone PARylation factor (HPF1) modulates the activity of PARP1/2 by forming a transient joint active site with them. The review discusses the discovery and classical mechanism of PARylation in higher eukaryotes, as well as the role of HPF1 in this process.
Article
Biochemistry & Molecular Biology
Chuanchao Zhang, Bo Zhou, Feng Gu, Hongmei Liu, Honglin Wu, Fuwen Yao, Hui Zheng, Hui Fu, Wei Chong, Shurui Cai, Min Huang, Xiaolu Ma, Zhifang Guo, Tingting Li, Wenyuan Deng, Meiwen Zheng, Qiao Ji, Yongliang Zhao, Yongjie Ma, Qi-En Wang, Tie-Shan Tang, Caixia Guo
Summary: This study identifies a human long noncoding RNA (lncRNA)-derived micropeptide, PACMP, which functions to maintain CtIP abundance and promote poly(ADP-ribosyl)ation. Targeting PACMP inhibits tumor growth through synthetic lethal interaction between CtIP and PARP inhibitions, and enhances sensitivity to various anticancer drugs and radiation.
Article
Biochemistry & Molecular Biology
Dongsheng Yao, Marcus A. Arguez, Ping He, Andrew F. Bent, Junqi Song
Summary: PARylation and K63-linked ubiquitination coordinately regulate plant immunity, with the PARylation of UBC13 regulating K63-linked ubiquitination of PDIs, which may further promote correct protein folding and secretion of PDIs.
Article
Biology
Pierre-Olivier Esteve, Sagnik Sen, Udayakumar S. Vishnu, Cristian Ruse, Hang Gyeong Chin, Sriharsa Pradhan
Summary: SET8, the enzyme responsible for H4K20me1, is post-translationally poly ADP-ribosylated by PARP1, leading to its degradation and aberrant H4K20 methylation. This regulation plays important roles in mitotic condensation, DNA replication, DNA damage response, and gene expression.
COMMUNICATIONS BIOLOGY
(2022)