Towards understanding the function of stress-inducible PtdIns(4,5)P(2) in plants.

The phosphoinositide (PI) system has been conserved in evolution between all eukaryotic kingdoms. Studies on mammalian and yeast cells indicate that cellular functions regulated by PIs include the production of soluble inositolpolyphosphates with signaling functions as well as recruitment of proteins required for endo- or exocytosis. In contrast to other models, knowledge on PI functions in plants is limited and, despite of reports of transient PI-increases upon stress-treatments, plant cellular processes involving changes in PI-levels have remained unclear. In previous studies various groups have proposed that PI-increases upon hyperosmotic stress support the generation of soluble second messengers with possible roles in stress adaptation. Based on a combination of biochemical analysis and imaging of fluorescent reporters we have now demonstrated that intact phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P(2)) associates with clathrin-coated vesicles (CCVs) in a stress-inducible manner in plant cells. In analogy to previous studies on other models, association with CCVs suggests a role for PtdIns(4,5)P(2) in the recruitment of vesicle coat proteins and in membrane internalization that is alternative to functions in second messenger production. The determination of subcellular sites of PtdIns(4,5)P(2) increases, thus, opens new avenues of investigation in the plant PI-field and allows development of testable hypotheses to delineate PI-functions in plants.