HSPA14 Activators

Given the nature of HSPA14 as a heat shock protein, it is logical to deduce that chemicals causing cellular stress might indirectly enhance its functional activity. For instance, Salubrinal, a selective inhibitor of eIF2α dephosphorylation, leads to accumulation of unfolded proteins, which in turn could necessitate increased activity of chaperone proteins such as HSPA14. Similarly, Eeyarestatin I, which inhibits ER-associated protein degradation (ERAD), could increase the demand for HSPA14 activity by causing an accumulation of misfolded proteins in the ER.

Moreover, disruption in protein transport from the ER to the Golgi apparatus by Brefeldin A could potentially increase the demand for HSPA14. Other compounds, like methotrexate and azetidine-2-carboxylic acid, which disrupt DNA synthesis and repair, or lead to the incorporation of incorrect amino acids into proteins, respectively, could potentially increase the demand for HSPA14. This logical analysis, although based on the known functions of HSPA14, should be validated by further experimental studies.