Specifically, when Caenorhabditis elegans larvae are infected by Pseudomonas aeruginosa, activation of the p38 MAPK family member 1 (PMK-1 -mediated PMK-1 -mediated induces IRE1/XBPMK-1 -mediated
To determine if PMK-3 functions in the same cells as GLR-1, we made a transgene, Pglr-1:: pmk-3, containing pmk-3 cDNA sequences (with mRFP sequences fused in frame at the PMK-3 N-terminus) under the control of the glr-1 promoter.
To give a second example, unlike sek-1 and nsy-1, pmk-1 does not have a role in neuronal development [21].
Unlike animals expressing Pglr-1::pmk-3, animals expressing Pglr-1::dlk-1 accumulated GLR-1 accretions in their neurites (data not shown).
We introduced Pglr-1::pmk-3 into pmk-3 lin-10 double mutants and found that mutant animals carrying the transgenic array had their GLR-1 localization defects restored (Fig. 4I), indicating that RFP PMK-3 can function cell autonomously.
To determine if the levels of PMK-3 are limiting, we introduced the Pglr-1::pmk-3 transgene into animals that also contained both wild-type alleles of the endogenous pmk-3 locus.
To examine PMK-3 subcellular localization, we introduced Pglr-1::pmk-3 into wild-type animals expressing GLR-1 GFP, GLR-1 GFPthandRfoundMK-3 prothat was localized to inteRFP PMK-3clei (Fig. 5C) and was pRFP PMK-3roughout the ventral cord neurites (Fig. 5D).
We generated lin-10 pmk-3 unc-11 triple mutants and examined GLR-1 accumulation.
Similarly, we depressed endocytosis in lin-10 pmk-3 double mutants by introducing the Pglr-1::rab-5(GDP) transgene.
The nsy-1 sek-1 pmk-1 cascade of p38 MAPK signaling is essential in the environmental response in C. elegans.
VHP-1 is a dual-specificity phosphatase that interacts with multiple MAP kinases including KGB-1, PMK-3, and PMK-1 [ 40- 42] and plays a role in modulating the respective signaling pathways during response to stress.
