Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/86549
Title: Endoplasmic reticulum - plasma membrane crosstalk mediated by the extended synaptotagmins
Authors: Saheki, Yasunori
Keywords: Ca2+
E-Syts
Non-vesicular lipid transport
Issue Date: 2017
Publisher: Springer, Singapore
Source: Saheki Y. (2017) Endoplasmic Reticulum – Plasma Membrane Crosstalk Mediated by the Extended Synaptotagmins. In: Tagaya M., Simmen T. (eds) Organelle Contact Sites. Advances in Experimental Medicine and Biology, vol 997. Springer, Singapore
Abstract: The endoplasmic reticulum (ER) possesses multiplicity of functions including protein synthesis, membrane lipid biogenesis, and Ca2+ storage and has broad localization throughout the cell. While the ER and most other membranous organelles are highly interconnected via vesicular traffic that relies on membrane budding and fusion reactions, the ER forms direct contacts with virtually all other membranous organelles, including the plasma membrane (PM), without membrane fusion. Growing evidence suggests that these contacts play major roles in cellular physiology, including the regulation of Ca2+ homeostasis and signaling and control of cellular lipid homeostasis. Extended synaptotagmins (E-Syts) are evolutionarily conserved family of ER-anchored proteins that tether the ER to the PM in PM PI(4,5)P2-dependent and cytosolic Ca2+-regulated manner. In addition, E-Syts possess a cytosolically exposed lipid-harboring module that confers the ability to transfer/exchange glycerolipids between the ER and the PM at E-Syts-mediated ER-PM contacts. In this chapter, the functions of ER-PM contacts and their role in non-vesicular lipid transport with special emphasis on the crosstalk between the two bilayers mediated by E-Syts will be discussed.
URI: https://hdl.handle.net/10356/86549
http://hdl.handle.net/10220/44092
ISBN: 978-981-10-4566-0
DOI: http://dx.doi.org/10.1007/978-981-10-4567-7_6
Rights: © 2017 Springer Nature Singapore Pte Ltd. This is the author created version of a work that has been peer reviewed and accepted for publication by Organelle Contact Sites, Springer Nature Singapore Pte Ltd. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://dx.doi.org/10.1007/978-981-10-4567-7_6].
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:LKCMedicine Books & Book Chapters

Google ScholarTM

Check

Altmetric

Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.