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. 2019 Apr 26;7:61. doi: 10.3389/fcell.2019.00061

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Copyright © 2019 Didiasova, Schaefer and Wygrecka.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Vacuole-related functions of ENO. Vacuole-associated ENO in parasites exists in three different variants: the low (50 and 65 kDa) and high (75 kDa) molecular weight forms. While the low molecular weight ENO variants regulate fusion of food vacuoles, the 75 kDa form interacts with hemozoin, a disposal product of hemoglobin digestion. Binding of ENO to hemozoin plays a role in parasites survival. In plants, ENO binds to subunits of the vacuolar H⁺-ATPase and V-ATPase and stimulates V-ATPase activity in an aldolase (ALD)-dependent manner by increasing the affinity for ATP. This mechanism is used by plants to overcome high salt concentrations.