Suppression of cell cycle progression by poly(ADP-ribose) polymerase inhibitor PJ34 in neural stem/progenitor cells

Kurokawa, Shu; Okuda, Akiko; Nishizawa, Yuki; Furukawa, Kyoko; Sumihiro, Ayumi; Nakaji, Yuki; Tanaka, Seigo; Takehashi, Masanori

doi:10.1016/j.bbrc.2019.01.025

Cited by 4 publications

(1 citation statement)

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“…PAR binders participate in the regulation of cell cycle progression, genome maintenance and transcription regulation [100,101]. Stalled replication forks activate PARP1, followed by PAR formation and S-phase checkpoint activation.…”

Section: Par-binding Proteins and Their Functionsmentioning

confidence: 99%

The Enigmatic Function of PARP1: From PARylation Activity to PAR Readers

Kamaletdinova

Fanaei-Kahrani

Wang

2019

Cells

111

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Poly(ADP-ribosyl)ation (PARylation) is catalysed by poly(ADP-ribose) polymerases (PARPs, also known as ARTDs) and then rapidly removed by degrading enzymes. Poly(ADP-ribose) (PAR) is produced from PARylation and provides a delicate and spatiotemporal interaction scaffold for numerous target proteins. The PARylation system, consisting of PAR synthesizers and erasers and PAR itself and readers, plays diverse roles in the DNA damage response (DDR), DNA repair, transcription, replication, chromatin remodeling, metabolism, and cell death. Despite great efforts by scientists in biochemistry, cell and molecular biology, genetics, and pharmacology over the last five decades, the biology of PARPs and PARylation remains enigmatic. In this review, we summarize the current understanding of the biological function of PARP1 (ARTD1), the founding member of the PARP family, focusing on the inter-dependent or -independent nature of different functional domains of the PARP1 protein. We also discuss the readers of PAR, whose function may transduce signals and coordinate the cellular processes, which has recently emerged as a new research avenue for PARP biology. We aim to provide some perspective on how future research might disentangle the biology of PARylation by dissecting the structural and functional relationship of PARP1, a major effector of the PARPs family.

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Section: Par-binding Proteins and Their Functionsmentioning

confidence: 99%