HSP90B1
Description
The HSP90B1 (heat shock protein 90 beta family member 1) is a protein-coding gene located on chromosome 12.
Heat shock protein 90kDa beta member 1 (HSP90B1), also known as endoplasmin, gp96, grp94, or ERp99, is a chaperone protein encoded by the HSP90B1 gene in humans. It is a paralogue of HSP90 found in the endoplasmic reticulum and plays a crucial role in folding proteins in the secretory pathway, including Toll-like receptors and integrins. HSP90B1 is considered an essential immune chaperone, regulating both innate and adaptive immunity. Tumor-derived HSP90B1 (vitespen) is being investigated in clinical trials for cancer immunotherapy. grp94 has been identified as a target for treating various diseases, such as glaucoma, multiple myeloma, and metastatic cancer. It possesses two unique sub-pockets, S1 and S2, formed by five distinct amino acids in its primary sequence. These sub-pockets are being explored in research efforts to inhibit the chaperone's activity, as its client proteins are often upregulated in cancer cells.
HSP90B1 is a molecular chaperone that aids in the processing and transport of secreted proteins. It is essential for the proper folding of Toll-like receptors when associated with CNPY3. Additionally, HSP90B1 participates in endoplasmic reticulum-associated degradation (ERAD). It has ATPase activity and may be involved in unfolding cytosolic leaderless cargos, such as interleukin 1, to facilitate their translocation into the ERGIC and subsequent secretion, a process mediated by the cargo receptor TMED10.
HSP90B1 is also known as ECGP, GP96, GRP94, HEL-S-125m, HEL35, TRA1.
