The Arabidopsis Synaptotagmin1 Is Enriched in Endoplasmic Reticulum-Plasma Membrane Contact Sites and Confers Cellular Resistance to Mechanical Stresses. Issue 1 (19th March 2015)
- Record Type:
- Journal Article
- Title:
- The Arabidopsis Synaptotagmin1 Is Enriched in Endoplasmic Reticulum-Plasma Membrane Contact Sites and Confers Cellular Resistance to Mechanical Stresses. Issue 1 (19th March 2015)
- Main Title:
- The Arabidopsis Synaptotagmin1 Is Enriched in Endoplasmic Reticulum-Plasma Membrane Contact Sites and Confers Cellular Resistance to Mechanical Stresses
- Authors:
- Pérez-Sancho, Jessica
Vanneste, Steffen
Lee, Eunkyoung
McFarlane, Heather E.
Esteban del Valle, Alicia
Valpuesta, Victoriano
Friml, Jiří
Botella, Miguel A.
Rosado, Abel - Abstract:
- Abstract : A phospholipid binding protein is enriched on specific organelle contact sites and maintains the mechanical stability of plant cells upon stress exposure. Abstract: 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 Ca 2+ 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.
- Is Part Of:
- Plant physiology. Volume 168:Issue 1(2015)
- Journal:
- Plant physiology
- Issue:
- Volume 168:Issue 1(2015)
- Issue Display:
- Volume 168, Issue 1 (2015)
- Year:
- 2015
- Volume:
- 168
- Issue:
- 1
- Issue Sort Value:
- 2015-0168-0001-0000
- Page Start:
- 132
- Page End:
- 143
- Publication Date:
- 2015-03-19
- Subjects:
- Plant physiology -- Periodicals
Botany -- Periodicals
Periodicals
Electronic journals
571.2 - Journal URLs:
- https://academic.oup.com/plphys/issue ↗
http://www.plantphysiol.org/ ↗
http://www.jstor.org/journals/00320889.html ↗
http://www.pubmedcentral.nih.gov/tocrender.fcgi?journal=69 ↗
http://www-us.ebsco.com/online/direct.asp?JournalID=101725 ↗
http://www.oxfordjournals.org/ ↗ - DOI:
- 10.1104/pp.15.00260 ↗
- Languages:
- English
- ISSNs:
- 0032-0889
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 16199.xml