# Exploring the Role of the Processing Body in Plant Abiotic Stress Response
## 3 Assembly of P-Body
### RNA Decay Is the Main Reason for the Formation of P-Body  
In cells, the P-Body mainly performs the degradation and storage functions of mRNA and plays a crucial role in the silencing and decay of mRNA [47]. Therefore, the formation and disassembly of the P-Body are directly related to the mRNA in the cytoplasm. When cells are in a specific growth stage or under stress conditions, a large amount of mRNA often appears in the cytoplasm. These mRNAs will participate in the formation of P-Bodies and promote the growth of the number and volume of P-Bodies. For example, the P-Bodies begin to increase in number as the cell approaches the S phase of cytokinesis until the end of interphase, and then breaks down during mitosis [48]. This may be because during the S phase of cell division, the transcription rate is very high, necessitating the involvement of the P-Body in mRNA degradation to regulate the quantity of mRNA and precisely control protein synthesis [48,49]. However, during cell division, the P-Body disassembles to ensure there is sufficient mRNA to rapidly translate and synthesize proteins to support cell growth once cell division is complete [48].  
Under stress conditions, in order to preferentially translate more new stress-related mRNAs, cells will inhibit the translation of some mRNAs that are not favorable to the stress response or are not suitable for mass translation under stress conditions. These mRNAs are involved in the formation of the P-Body and are then degraded or stored in the P-Body. When the cell's growth environment returns to normal conditions, the P-Body in the cytoplasm breaks down, and the mRNAs stored in the P-Body return to the ribosomes to be translated again. The cell's mRNAs that have been repressed in the cytoplasm are then degraded and stored in the P-Body, and the mRNAs that have been repressed are then returned to the ribosomes for translation [4]. In addition, the P-Body can also resist RNA virus infection of cells through the mRNA degradation pathway. At the same time, the P-Body is also the target of RNA virus attacks. [PERSON] et al. used three RNA viruses, SARS-CoV-2, OC43, and 229E, to infect human umbilical vein endothelial cells (HUVECs) for 24 h and found that the amount of P-Body in the cytoplasm was significantly reduced [50]. It is worth noting that while the P-Body is depolymerized, inflammatory cytokine transcripts will also return to cytoplasmic ribosomes for translation, thereby alerting and activating the immune system to enhance resistance to viruses [50]. The aforementioned results indicate that the formation of P-Bodies is related to RNA decay. Additionally, studies have shown that the aggregation of P-Body components is associated with the microtubule network, an essential structure of the cytoskeleton. [PERSON] et al. discovered that disrupting the microtubules of yeast cells with 15 ug/mL benomyl for 60 min led to an increase in the levels of P-Body proteins such as Dhh1p, Dcp2p, and Xrn1, subsequently leading to the aggregation and formation of P-Bodies [50, 51, 52]. Notably, the disruption of cellular microtubules does not result in the inhibition of mRNA translation [51]. At present, it is not clear why damaging cellular microtubules leads to P-Body aggregation, but it may be related to the fact that microtubules restrict the movement of P-Bodies [49].