Short NoteSimilar dose response of heat shock protein synthesis and intracellular pH change in yeast
References (14)
- et al.
Cell
(1979) - et al.
Exp cell res
(1974) - et al.
Exp cell res
(1975) - et al.
Heat-shock from bacteria to man
(1982) - et al.
Current genet
(1979) Nature
(1975)- et al.
Subcell biochem
(1974)
Cited by (61)
Condensation of Ded1p Promotes a Translational Switch from Housekeeping to Stress Protein Production
2020, CellCitation Excerpt :Although the condensates formed at low pH were spherical, condensates formed at elevated temperature resembled clusters of small spherical structures, suggesting that they form by phase separation but then gel rapidly. Heat-shocked cells experience a decrease in cytosolic pH to approximately 6.5 (Kroschwald et al., 2018; Weitzel et al., 1985). We thus tested for the effect of pH on temperature-induced Ded1p condensation.
Cellular sensing by phase separation: Using the process, not just the products
2019, Journal of Biological ChemistryCitation Excerpt :Unlike the two-dimensional phase diagram shown in Fig. 1C, a phase diagram for a biomolecule may have multiple dimensions, each of which can be modulated to regulate phase behavior. For example, the intracellular environment of yeast undergoes dynamic changes when the cell encounters stress: the cellular ATP level drops (38); the intracellular pH drops by 0.5–1 pH unit (39–41); the cellular volume shrinks and the intracellular environment becomes more crowded (42); and the cytoplasm transitions from viscous fluid to a more glass-like state (39, 42). These parameters—concentrations of specific mRNAs, ATP, protons, and crowders—have been demonstrated to affect the phase boundaries of proteins that undergo phase separation (24, 43–48).
Effect of handling, confinement and crowding in HSP70 production in Pachygrapsus marmoratus, a model species for climate change experiments
2012, Journal of Sea ResearchCitation Excerpt :However, a complete understanding of the mechanisms underlying the regulation of HSP70s is far from clear (Iwama et al., 2004). Although HSP70 are very sensitive to temperature, their production can also be stimulated by other factors like hypoxia (Dwyer et al., 1989; Guttman et al., 1980; Iwaki et al., 1993), energy depletion (Sciandra and Subjeck, 1983), acidosis (Weitzel et al., 1985), reactive oxygen species formation (Wallen et al., 1997) and acute exercise (Locke et al., 1990; Skidmore et al., 1995). In an effort to understand the mechanisms underlying HSP70 expression with temperature increase, we designed a series of parallel experiments with Pachygrapsus marmoratus (Grapsidae), where the effect of temperature was concomitantly tested with other factors such as size, sex, pH and salinity (unpublished work).
Geranylgeranylaceton induces heat shock protein 72 in skeletal muscle cells
2007, Biochemical and Biophysical Research CommunicationsCitation Excerpt :It is well known that HSP72, the inducible form of HSP70, is up-regulated by exposure to heat [9,10,16,17]. Up-regulation of HSP72 is induced by not only heat-stress but also many types of cellular stresses, such as the reduced peripheral blood circulation, oxygen radicals, and/or H+[9,18–21]. The HSP72 function as an important molecular chaperone [22,23].
Agglomeration: when folded proteins clump together
2023, Biophysical ReviewsA brief guideline for studies of phase-separated biomolecular condensates
2022, Nature Chemical Biology