# Exploring the Role of the Processing Body in Plant Abiotic Stress Response
## 5 Conclusions and Perspectives  
The P-Body responds to abiotic stresses in plant cells such as drought, salt, and temperature stress by regulating mRNA uncapping, degradation, translational repression, and storage at the post-transcriptional level. It also improves plant stress resistance by being involved in ethylene signaling pathways [8]. The formation of the P-Body is related to mRNA decay. Under stress conditions, plant cells prioritize the translation of mRNAs that favor the stress response by inhibiting the translation of transcripts that are less favorable [4]. These non-translating mRNAs form P-Bodies through liquid-liquid phase separation (LLPS) with proteins containing intrinsically disordered regions (IDRs), low-complexity sequences, RNA-binding activities, or prion-like domains, and are either stored within them or degraded [19,31]. In addition to mRNA that is unfavorable to the stress response, aberrant mRNA is also degraded by P-Bodies. It is worth noting that mRNA that is beneficial to stress response, such as the mRNA of heat stress transcription factors (HSFs), is also stored in the P-Body to prevent degradation [28]. The proteins of the P-Body can be categorized into conserved proteins and dynamic proteins. DCP1, DCP2, DCP5, VCS, and XRN4 are conserved proteins of the P-Body and play crucial roles in the 5\({}^{\prime}\)\(\rightarrow\)3\({}^{\prime}\) degradation process of mRNA [10,22]. Abiotic stresses activate kinase MPK6 and SnRK2 to phosphorylate DCP1 and VCS, respectively, promoting DCP1, DCP2, DCP5, and VCS to form decapping complexes to excise the 5\({}^{\prime}\)-m7 Gpp protecting structure of mRNAs unfavorably resistant or aberrantly transcribed [55,56]. And the decapped mRNA is subsequently degraded by 5\({}^{\prime}\)\(\rightarrow\)3\({}^{\prime}\) exoribonuclease XRN4 (Figure 1) [60]. It is interesting to note that under biotic stress, in plant cell pattern recognition receptors (PRR)-mediated plant immunity against pathogens, MPK6 also phosphorylates DCP1, but the 5\({}^{\prime}\)\(\rightarrow\)3\({}^{\prime}\) degradation process of mRNAs changes. [PERSON] et al. found that the flg22, known to induce this immune response, activates the kinases MPK3 and MPK6 when entering cells. The MPK3 and MPK6 phosphorylate DCP1 when the mRNA is decapped by the decapping complex in P-Body. The phosphorylated DCP1 then dissociates from the decapping complex and associates with the nucleic acid exonuclease XRN4 [71]. The association of phosphorylated DCP1 with XRN4 may further promote the degradation of mRNA by the nucleic acid exonuclease XRN4. This may indicate that the role of MPK6 in phosphorylating DCP1 is different under abiotic and biotic stresses. Under abiotic stress, MPK6 promotes the formation of a decapping complex of DCP1 with DCP2 and DCP5 to promote mRNA decapping and the formation of the P-Body. In contrast, under biotic stress, MPK6 promotes the detachment of DCP1 from the decapping complex and its association with the nucleic acid exonuclease XRN4, which promotes the degradation of decapitated mRNA and the disassembly of the P-Body. The disassembly of the P-Body plays an important role in plant immune responses under biotic stress. The above phenomenon suggests that the assembly and disassembly of the P-Body is a result of the different functions performed by the components of P-Body, reflecting the dynamic nature of membrane-less organelles such as the P-Body. Besides mRNA degradation, the P-Body might also inhibit translation and store the mRNA under stresses. This facilitates the rapid translation of mRNAs required for plant growth to adapt to normal environments and protect mRNAs functionally involved in the stress response (Figure 1). Currently, the dynamic protein composition of the P-Body remains unclear. This is due to the fact that the components of the P-Body are affected by factors such as cell type, growth period, and external environmental stress, showing a complex and dynamic regulatory mechanism.