ROSY1, a novel regulator of gravitropic response is a stigmasterol binding protein.

Autor: Dalal J; Dept. of Plant and Microbial Biology, North Carolina State University, Raleigh, NC 27695-7621, United States., Lewis DR; Dept. of Biology, Wake Forest University, Winston-Salem, NC 27109, United States., Tietz O; University of Freiburg, Germany., Brown EM; Dept. of Plant and Microbial Biology, North Carolina State University, Raleigh, NC 27695-7621, United States., Brown CS; Dept. of Plant and Microbial Biology, North Carolina State University, Raleigh, NC 27695-7621, United States., Palme K; University of Freiburg, Germany., Muday GK; Dept. of Biology, Wake Forest University, Winston-Salem, NC 27109, United States., Sederoff HW; Dept. of Plant and Microbial Biology, North Carolina State University, Raleigh, NC 27695-7621, United States. Electronic address: hwsedero@ncsu.edu.
Jazyk: angličtina
Zdroj: Journal of plant physiology [J Plant Physiol] 2016 Jun 01; Vol. 196-197, pp. 28-40. Date of Electronic Publication: 2016 Mar 24.
DOI: 10.1016/j.jplph.2016.03.011
Abstrakt: The gravitropic bending in plant roots is caused by asymmetric cell elongation. This requires an asymmetric increase in cell surface and therefore plasma membrane components such as lipids, sterols, and membrane proteins. We have identified an early gravity-regulated protein in Arabidopsis thaliana root apices that binds stigmasterol and phosphoethanolamines. This root-specific protein interacts with the membrane transport protein synaptotagmin-1 and was therefore named InteractoR Of SYnaptotagmin1 (ROSY1). While interactions between ML-domain proteins with membrane transport proteins and their impact have been reported from animal cell systems, this is the first report of such an interaction in a plant system. Homozygous mutants of ROSY1 exhibit decreased basipetal auxin transport, a faster root gravitropic response, and an increase in salt stress tolerance. Our results suggest that ROSY1 plays a role in root gravitropism, possibly by facilitating membrane trafficking and asymmetric cell elongation via its interaction with synaptotagmin-1.
(Copyright © 2016 The Authors. Published by Elsevier GmbH.. All rights reserved.)
Databáze: MEDLINE
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