HSP90 in morphogenesis: taking the heat and keeping the dark Protein homeostasis (proteostasis) is essential for the proper functioning of all individual cells, as well as maintaining the correct dynamic between neighboring cells. While there are a number of mechanisms in place to achieve this, one of the most common is the Hsp70/Hsp90 molecular chaperone system (Taipale et al., 2010). HSP90 is a highly abundant and central cellular component essential to the maturation and stabilization of numerous substrate proteins (clients). These clients are often regulatory proteins involved in signaling pathways. The range of processes and types of client proteins that HSP90 regulates are many and varied, ranging from various biotic and abiotic stresses to hormone signaling and the circadian clock (Kim et al., 2011;di Donato & Geisler, 2019). For example, stem elongationthrough the action of auxin, a primary hormone involved in cell expansionindirectly requires the function of HSP90 through the HSP90-mediated stabilization of the auxin coreceptor F-box protein, TIR1 (Wang et al., 2016). However, in an article published in this issue of New Phytologist, Zeng et al. (2023; pp. 1253-1265 now report a new, specific role for HSP90 as a direct participant in the regulation of dark-grown seedling development (skotomorphogenesis) and thermomorphogenesis, through effects on ELF3 levels.