Hsp90b1, also known as gp96 or Grp94, is a conserved member of the heat shock protein family and acts as a molecular chaperone for oncogenes, playing crucial roles in protein folding and translocation [1,3]. It is involved in multiple pathways, such as those related to tumor metabolism, cell cycle, and immune checkpoint regulation [1].

In cancer research, Hsp90b1 has been found to be highly expressed in various tumors, often correlating with poor prognosis. For example, in NSCLC patients, its overexpression is an independent poor prognostic factor for overall survival and disease-free survival [4]. In glioblastoma, it promotes the plasma membrane localization of GLUT1, enhancing glycolytic activity, tumor growth, and radioresistance [2]. In gastric cancer, it forms a positive feedback loop with LINC00501 and STAT3, promoting malignant behavior [5]. Also, the HSP90B1 inhibitor PU-WS13 can suppress cancer cell proliferation and reduce the expression of PD-L1 [1]. In the context of tuberculosis, HSP90B1 gene-region variants are associated with BCG-induced IL-2 production and may be related to protection from TB disease [6].

In conclusion, Hsp90b1 is a significant gene involved in protein-related biochemical processes. Its high expression in various cancers and association with poor prognosis, as well as its role in promoting tumor-related activities, make it a potential target for cancer diagnosis, prognosis, and therapy. In addition, its role in the immune response to Mycobacteria indicates its importance in infectious disease-related immunity [1,2,4,5,6].