What is it about?
We have previously described that the phosphoinositide kinase PIP5K6 can be phosphorylated in pollen tubes by the MAPK MPK6. Here we provide evidence that this phosphorylation event is triggered by sensing bacterial flagellin at the cell surface and that phosphoinositide-mediated cellular functions are consequentially affected. Our data, thus, expand the understanding of this regulatory step both in the upstream and downstream direction.
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Why is it important?
Our work indicates a new link between two ancient eukaryotic signaling pathways, mitogen-activated protein kinases (MAPKs) and phosphoinositides (PIs). The observation suggests new roles of MAPK signaling in the control of cytoplasmic processes, including membrane trafficking and possibly cytoskeletal dynamics.
Perspectives
It remains currently unclear how relevant the particular effect on PIP5K6 will be, as the importantce and exact physiological role of this enzyme remains unknown. It is possible that a key important finding of our study is in the difference between the MAPK-dependent control of PIP5K6 and the MAPK-independent function of other PI4P 5-kinases, such as PIP5K2, indicating that PI4P 5-kinase isoforms are subject to independent modes of regulation.
Ingo Heilmann
Martin-Luther-Universitat Halle-Wittenberg
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This page is a summary of: A PAMP‐triggered MAPK‐cascade inhibits phosphatidylinositol 4,5‐bisphosphate production by PIP5K6 in
Arabidopsis thaliana, New Phytologist, July 2019, Wiley,
DOI: 10.1111/nph.16069.
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