High impact information on HSP42

• In contrast to Hsp26, which functions predominantly at heat shock temperatures, Hsp42 is active as a chaperone under all conditions tested in vivo and in vitro [1].
• Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae [1].
• Taken together, our results define Hsp42 as an important player for protein homeostasis at physiological and under stress conditions [1].
• Yeast in which the HSP42 gene was disrupted and which was subjected to moderate thermal stress reorganized the actin cytoskeleton more slowly than did wild-type control cells [2].
• Expression of HSP42, the gene for a small heat shock protein (sHSP), from a high-copy-number plasmid reversed this effect [2].

Biological context of HSP42

• The small heat shock proteins, Hsp26 and Hsp42, also function in the recovery of misfolded proteins and prevent aggregation in vitro, but their in vivo roles in protein homeostasis remain elusive [3].

Anatomical context of HSP42

• We demonstrate, that Hsp42 is expressed in inclusion bodies and can be resolubilized and folded to correct, active oligomers [4].

Associations of HSP42 with chemical compounds

• Induction of HSP42 by AZC treatment required protein synthesis; treatment with ethanol, which can also misfold proteins, activated heat shock factor, but treatment with canavanine, an arginine analog less potent than AZC at misfolding proteins, did not [5].

Regulatory relationships of HSP42

• Expression of HSP42 is regulated by a range of stress conditions similar to S. cerevisiae HSP26, with which Hsp42p shares most homology [6].

Other interactions of HSP42

• However, HSP42 expression is more sensitive to increased salt concentration and to starvation and, in contrast to HSP26 is expressed in unstressed cells [6].

Analytical, diagnostic and therapeutic context of HSP42

• Hsp42p interacts with itself in the two-hybrid assay [6].

References