Homomeric interaction of AtVSR1 is essential for its function as a vacuolar sorting receptor.

Plant Physiology
Hyeran KimInhwan Hwang

Abstract

Vacuolar sorting receptors, BP80/VSRs, play a critical role in vacuolar trafficking of soluble proteins in plant cells. However, the mechanism of action of BP80 is not well understood. Here, we investigate the action mechanism of AtVSR1, a member of BP80 proteins in Arabidopsis (Arabidopsis thaliana), in vacuolar trafficking. AtVSR1 exists as multiple forms, including a high molecular mass homomeric complex in vivo. Both the transmembrane and carboxyl-terminal cytoplasmic domains of AtVSR1 are necessary for the homomeric interaction. The carboxyl-terminal cytoplasmic domain contains specific sequence information, whereas the transmembrane domain has a structural role in the homomeric interaction. In protoplasts, an AtVSR1 mutant, C2A, that contained alanine substitution of the region involved in the homomeric interaction, was defective in trafficking to the prevacuolar compartment and localized primarily to the trans-Golgi network. In addition, overexpression of C2A, but not wild-type AtVSR1, inhibited trafficking of soluble proteins to the vacuole and caused their secretion into the medium. Furthermore, C2A:hemagglutinin in transgenic plants interfered with the homomeric interaction of endogenous AtVSR1 and inhibited vacuolar ...Continue Reading

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Citations

Sep 22, 2011·The Plant Cell·David ScheuringKarin Schumacher
Oct 9, 2014·The Plant Journal : for Cell and Molecular Biology·Jinbo ShenLiwen Jiang
Jun 7, 2013·The Plant Journal : for Cell and Molecular Biology·Jinbo ShenLiwen Jiang
Jun 5, 2016·Journal of Experimental Botany·David G Robinson, Jean-Marc Neuhaus
Oct 6, 2016·International Journal of Molecular Sciences·Alessandro OcchialiniJean-Marc Neuhaus
Jan 10, 2017·Journal of Cellular Biochemistry·Sung-Jin BaeKyu-Won Kim
Mar 22, 2018·Annual Review of Plant Biology·Tomoo ShimadaIkuko Hara-Nishimura
Nov 3, 2017·Journal of Experimental Botany·Gian Pietro Di SansebastianoCarine de Marcos Lousa

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