Functional Roles of Poly(ADP-Ribose) in Stress Granule Formation and Dynamics.

Xuejiao Jin,Xiuling Cao,Beidong Liu,Shenkui Liu

doi:10.3389/fcell.2021.671780

Abstract

Stress granules (SGs) are highly dynamic cytoplasmic foci formed in response to stress. The formation of SGs is reported to be regulated by diverse post-translational protein modifications (PTMs). Among them, ADP-ribosylation is of emerging interest due to its recently identified roles in SG organization. In this review, we summarized the latest advances on the roles of poly(ADP-ribose) (PAR) in the regulation of SG formation and dynamics, including its function in modulating nucleocytoplasmic trafficking and SG recruitment of SG components, as well as its effects on protein phase separation behavior. Moreover, the functional role of PAR chain diversity on dynamic of SG composition is also introduced. Potential future developments on investigating global ADP-ribosylation networks, individual roles of different PARPs, and interactions between ADP-ribosylation and other PTMs in SGs are also discussed.

Highlights

Stress granules (SGs) are cytoplasmic membraneless structures that rapidly assemble in cells in response to a variety of stresses, including heat, oxidative stress, and virus infection (Buchan and Parker, 2009)
In this mini-review, we focus on how ADP-ribosylation, an important protein modifications (PTMs), participates
Several studies have found that PAR is present in SGs, and that many proteins in SGs are PARylated or possess PAR-binding domains, such as heterogeneous nuclear ribonucleoprotein A1, TAR DNA binding protein 43 kDa (TDP-43), FIGURE 1 | Roles of poly(ADP-ribose) (PAR) in stress granules (SG) formation, composition, and dynamics

Summary

Introduction

Stress granules (SGs) are cytoplasmic membraneless structures that rapidly assemble in cells in response to a variety of stresses, including heat, oxidative stress, and virus infection (Buchan and Parker, 2009). Several studies have found that PAR is present in SGs, and that many proteins in SGs are PARylated or possess PAR-binding domains, such as heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1), TAR DNA binding protein 43 kDa (TDP-43), FIGURE 1 | Roles of poly(ADP-ribose) (PAR) in stress granules (SG) formation, composition, and dynamics.

Results

Conclusion