Rabs appear to be concentrated to specific subcellular compartments in eukaryotic cells. They are targeted to microdomains in specific organelles via interactions with their effectors. Reports have suggested that Rab7 plays a role in vesicular transport from early endosomes to late endosomes in the cytoplasm. The results of the subcellular localization of TaRab7 based on the transient assays showed that TaRab7 is located in both the cytoplasm and at the periphery of the nucleus. The gene transport materials in the cytoplasm and the location in perinuclear area suggest that the gene is BKM120 associated with lysosomes or plays a role in the regulation of the perinuclear lysosome compartment. In Hela cells, Rab7 was associated with lysosomes, which aggregated and fused in the perinuclear region. In the absence of a functional Rab7 protein, the lysosomes become dispersed. In this sense, Rab7 is a key regulatory protein for proper aggregation and fusion of late endocytic structures in the perinuclear region and consequently for the biogenesis and maintenance of the lysosomal compartment. Lysosomes of most cells function principally in intracellular digestion and contain several enzymes, mainly acid hydrolases, and the function of lysosomes is not restricted to protein degradation; they also fuse with the plasma membrane during cell injury, as well as having more specialized secretory functions in some cell types. Nascent phagosomes must undergo a series of fusion and fission reactions to acquire the microbicidal properties required for the innate immune response. Here reports demonstrate that this maturation process involves the GTPase Rab7. Rab7 recruitment to phagosomes was found to precede and to be essential for their fusion with late endosomes and/or lysosomes. Active Rab7 on the phagosomal membrane associates with the effector protein RILP, which in turn bridges phagosomes with dyneindynactin, a microtubule-associated motor complex. RILP has been studied because it can be recruited efficiently on late endosomal and lysosomal membranes by Rab7GTP. And this may explain one function of TaRab7 in wheat against the pathogen. When some pathogens invade the plant, they secrete some materials into plant cells that facilitate infection. Accordingly, TaRab7 may regulate lysosome and phagosomes to render these toxic materials dysfunctional. The explanation for localization of TaRab7 in the nucleus requires further examination. Following the demonstration of the pivotal role of TaRab7 in wheat defense response, dissecting of its signaling pathway, such as identifying its upstream regulators, downstream effectors, and interacting or interconnected partners becomes the next major task. Transcriptomic analyses have highlighted differences in intestinal gene expression patterns between samples collected from patients with inflammatory bowel disease compared to control patients without inflammatory bowel disease. Differences in transcript levels, particularly those involved in inflammatory pathways, have been observed.