4.8 Article

The Arabidopsis Synaptotagmin1 Is Enriched in Endoplasmic Reticulum-Plasma Membrane Contact Sites and Confers Cellular Resistance to Mechanical Stresses

Journal

PLANT PHYSIOLOGY
Volume 168, Issue 1, Pages 132-U837

Publisher

AMER SOC PLANT BIOLOGISTS
DOI: 10.1104/pp.15.00260

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Funding

  1. Formacion del Personal Investigador Fellowship from the Ministerio de Economia y Competitividad [FPI-BES 2012-052324]
  2. Ministerio de Ciencia e Innovacion
  3. European Regional Development Fund [BIO2011-23859, P07-CVI-03021]
  4. Consejeria de Innovacion Ciencia y Empresa-La Junta de Andalucia
  5. postdoctoral research fellowship of the Research Foundation-Flanders
  6. Natural Sciences and Engineering Research Council of Canada Discovery [RGPIN-2014-06468]
  7. Canada Research Chairs programs

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Eukaryotic endoplasmic reticulum (ER)-plasma membrane (PM) contact sites are evolutionarily conserved microdomains that have important roles in specialized metabolic functions such as ER-PM communication, lipid homeostasis, and Ca2+ influx. Despite recent advances in knowledge about ER-PM contact site components and functions in yeast (Saccharomyces cerevisiae) and mammals, relatively little is known about the functional significance of these structures in plants. In this report, we characterize the Arabidopsis (Arabidopsis thaliana) phospholipid binding Synaptotagmin1 (SYT1) as a plant ortholog of the mammal extended synaptotagmins and yeast tricalbins families of ER-PM anchors. We propose that SYT1 functions at ER-PM contact sites because it displays a dual ER-PM localization, it is enriched in microtubule-depleted regions at the cell cortex, and it colocalizes with Vesicle-Associated Protein27-1, a known ER-PM marker. Furthermore, biochemical and physiological analyses indicate that SYT1 might function as an electrostatic phospholipid anchor conferring mechanical stability in plant cells. Together, the subcellular localization and functional characterization of SYT1 highlights a putative role of plant ER-PM contact site components in the cellular adaptation to environmental stresses.

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