Published in Journal of Experimental Botany 75, 14, 4274–4286. 2024.  

New Publication: "The role of the co-chaperone HOP in plant homeostasis during development and stress"

Proteins need to acquire their native structure in order to become fully functional. In specifc cases, the active conformation is obtained spontaneously; nevertheless, many proteins need the assistance of chaperones and co-chaperones to be properly folded.


These proteins help to maintain protein homeostasis under control conditions and under different stresses. HOP (HSP70–HSP90 organizing protein) is a highly conserved family of co-chaperones that assist
HSP70 and HSP90 in the folding of specifc proteins. In the last few years, fndings in mammals and yeast have revealed novel functions of HOP and re-defned the role of HOP in protein folding. Here, we provide an overview of the most important aspects of HOP regulation and function in other eukaryotes and analyse whether these aspects are conserved in plants. In addition, we highlight the HOP clients described in plants and the role of HOP in plant development and stress response.

Castellano MM,  Muñoz A, Okeke I,  Novo-Uzal E, Toribio R,  Mangano S. The role of the co-chaperone HOP in plant homeostasis during development and stressJournal of Experimental Botany 75, 14, 4274–4286. 2024.  https://doi.org/10.1093/jxb/erae013