Juvenile hormone membrane signaling phosphorylates Hsp83 and promotes Met nuclear import

ABSTRACT: JH modulates phosphorylation modification of components of its intracellular signaling through putative membrane pathway. As a transcriptional factor, Met phosphorylation is contributed to its transcriptional activity, but whether phosphorylation modification affects Met nuclear import is unknown. Here, we report that phosphorylation sites are dispensable for NLS activity whether JH is present or not. Interestingly, binding affinity of Met and Hsp83 fails to increase by adding JH is resulted from the mutant of JH-regulated phosphorylation of Hsp83 at S219. JH also increase binding affinity of Hsp83 and 14-3-3 proteins independent on S219. 14-3-3 proteins negatively regulated JH activity through sequestrating Met in the cytoplasm that dependent on Hsp83, which acts as a bridge between Met/Gce and 14-3-3 proteins. These results suggest that JH membrane pathway phosphorylates either Met or Hsp83 to promote JH intracellular signaling, meanwhile, a negative feedback loop forms between the 14-3-3 proteins and Hsp83.

ORGANISM(S): Drosophila Melanogaster

SUBMITTER: Sheng Li  

PROVIDER: PXD027314 | iProX | Thu Jul 15 00:00:00 BST 2021

REPOSITORIES: iProX