Structure and Function of TPC1 Vacuole SV Channel Gains Shape

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Plants and animals in endosomes operate TPC1/SV-type cation channels. All plants harbor at least one TPC1 gene. Although the encoded SV channel was firstly discovered in the plant vacuole membrane two decades ago, its biological function has remained enigmatic. Recently, the structure of a plant TPC1/SV channel protein was determined. Insights into the 3D topology has now guided site-directed mutation approaches, enabling structure–function analyses of TPC1/SV channels to shed new light on earlier findings. Fou2 plants carrying a hyperactive mutant form of TPC1 develop wounding stress phenotypes. Recent studies with fou2 and mutants that lack functional TPC1 have revealed atypical features in local and long-distance stress signaling, providing new access to the previously mysterious biology of this vacuolar cation channel type in planta. The biological function of endosomal TPC1/SV-type cation channels is controversially discussed. The structural data recently obtained provide novel insights into the biological role and evolution of these enigmatic ion channels.




Hedrich, R., Mueller, T. D., Becker, D., & Marten, I. (2018, June 4). Structure and Function of TPC1 Vacuole SV Channel Gains Shape. Molecular Plant. Cell Press.

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