MAPK phosphorylation is implicated in the adaptation to desiccation stress in nematodes

Abstract

SUMMARYSome nematodes can survive almost complete desiccation by entering an ametabolic state called anhydrobiosis requiring the accumulation of protective molecules such as trehalose and LEA proteins. However, it is not known how anhydrobiotic organisms sense and regulate the response to water loss. Mitogen-activated protein kinases (MAPKs) are highly conserved signalling proteins that regulate adaptation to various stresses. Here, we first compared the anhydrobiotic potential of three nematode species, Caenorhabditis elegans, Aphelenchus avenae and Panagrolaimus superbus, and then determined the phosphorylation status of the MAPKs p38, JNK and ERK during desiccation and rehydration. Caenorhabditis elegans was unable to undergo anhydrobiosis even after an initial phase of slow drying (preconditioning), while A. avenae did survive desiccation after preconditioning. In contrast, P. superbus withstood desiccation under rapid drying conditions, although survival rates improved with preconditioning. These results characterise C. elegans as desiccation sensitive, A. avenae as a slow desiccation strategist anhydrobiote and P. superbus as a fast desiccation strategist anhydrobiote. Both C. elegans and A. avenae showed increased MAPK phosphorylation during drying, consistent with an attempt to mount protection systems against desiccation stress. In P. superbus, however, MAPK phosphorylation was apparent prior to water loss and then decreased on dehydration, suggesting that signal transduction pathways are constitutively active in this nematode. Inhibition of p38 and JNK in P. superbus decreased its desiccation tolerance. This is consistent with the designation of P. superbus as a fast desiccation strategist and its high level of preparedness for anhydrobiosis in the hydrated state. These findings show that MAPKs play an important role in the survival of organisms during anhydrobiosis. Supplementary material available online at

A Rapid Transcriptome Response Is Associated with Desiccation Resistance in Aerially-Exposed Killifish Embryos

“…All three types of MAPKs (ERK, p38 and JNK) play a role during desiccation, oxidative and osmotic stress in a wide range of organisms, regardless of whether they are able to reach an anhydrobiotic stage and survive severe desiccation conditions [63], [64], [65]. In F. heteroclitus mid-gastrula embryos, MAPKs may also be involved in the sensing and transduction of desiccation since we observed that expression of genes that can potentially participate in the p38 MAPK and SAPK/JNK ( dusp23-like , stk39 , mink1-like ), and MAPK/ERK ( prkcbb , camk2d ), signaling pathways is strongly and transiently enhanced after 30 min-1 h of aerial incubation (Figure 3A).…”

“…Among these genes are those potentially involved in phosphorylation signaling pathways, oxidative stress or molecular chaperones [5], [65], [105], suggesting critical adaptations to survival in killifish embryos that may resemble to other species undergoing dormancy, diapause or desiccation. Thus, desiccation resistance during delayed hatching of killifish embryos may be an useful model to elucidate common and distinct pathways for the long term preservation of animal cells.…”

Screening and analysis of Hc-ubq and Hc-gst related to desiccation survival of infective Haemonchus contortus larvae

“…Slow desiccated nematodes such as Aphelenchus avenae, require a period of slow desiccation as pretreatment before they survive in extreme dryness (Tunnacliffe and Lapinski, 2003). Rapid desiccated nematodes are capable to directly enter anhydrobiosis without pretreatment, for example Panagrolaimus superbus (Banton and Tunnacliffe, 2012). Diapausing C. elegans belong to the slow desiccated nematodes.…”

MKK3 Was Involved in Larval Settlement of the Barnacle Amphibalanus amphitrite through Activating the Kinase Activity of p38MAPK

“…Alternatively, to confirm the phosphorylation of p38MAPK by MKK3 in vivo , reversely increased activation of MKK3 is expected in response to inhibition of p38MAPK through negative feedback regulation [42], [43]. SB203580 is widely implicated as a specific inhibitor of p38MAPK [17], [44]–[46]. It binds to an extended pocket in the active site of p38MAPK and blocks the formation of functional complexes with substrates [47].…”