Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/85553
Title: The Extended-Synaptotagmins
Authors: Saheki, Yasunori
De Camilli, Pietro
Keywords: Synaptotagmin
Tricalbin
Issue Date: 2017
Source: Saheki, Y., & De Camilli, P. (2017). The Extended-Synaptotagmins. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1864(9), 1490-1493.
Series/Report no.: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
Abstract: The extended-synaptotagmins (tricalbins in yeast) derive their name from their partial domain structure similarity to the synaptotagmins, which are characterized by an N-terminal membrane anchor and cytosolically exposed C2 domains. However, they differ from the synaptotagmins in localization and function. The synaptotagmins tether secretory vesicles, including synaptic vesicles, to the plasma membrane (PM) via their C2 domains and regulate their Ca2+ triggered exocytosis. In contrast, the extended-synaptotagmins are resident proteins of the endoplasmic reticulum (ER), which tether this organelle to the plasma membrane via their C2 domains, but not as a premise to fusion of the two membranes. They transport glycerolipids between the two bilayers via their lipid-harboring SMP domains and Ca2+ regulates their membrane tethering and lipid transport function. Additionally, the extended-synaptotagmins are more widely expressed in different organisms, as they are present not only in animal cells, but also in fungi and plants, which do not express the synaptotagmins. Thus, they have a more general function than the synaptotagmins, whose appearance in animal species correlated with the occurrence of Ca2+ triggered exocytosis. This article is part of a Special Issue entitled: Membrane Contact Sites edited by Christian Ungermann and Benoit Kornmann.
URI: https://hdl.handle.net/10356/85553
http://hdl.handle.net/10220/43754
ISSN: 0167-4889
DOI: http://dx.doi.org/10.1016/j.bbamcr.2017.03.013
Rights: © 2017 Elsevier B.V. This is the author created version of a work that has been peer reviewed and accepted for publication by Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, Elsevier B.V. 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/10.1016/j.bbamcr.2017.03.013].
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:LKCMedicine Journal Articles

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