Phosphatidylinositol-transfer proteins (PITPs) have been initially identified as soluble factors that accelerate the monomeric exchange of either phosphatidylinositol (PI) or phosphatidylcholine (PC) between membrane bilayers in vitro. They are highly conserved in eukaryotes and have been implicated in different cellular processes, including vesicular trafficking, signal transduction, and lipid metabolism. Recent studies suggest that PITPs function at membrane contact sites (MCSs) to facilitate the transport of PI from its synthesis site at the endoplasmic reticulum (ER) to various membrane compartments. In this review, we describe the underlying mechanism of PITPs targeting to MCSs, discuss their cellular roles and potential mode of action.
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April 2016
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Cover Image
Endoplasmic reticulumendosome contact sites. This pseudo-colored electron microscopy image shows the formation of inter-organelle membrane contact sites between late endosomes (magenta) and the endoplasmic reticulum (ER; green). This tethering results from the interaction between two ER-anchored proteins (VAP-A and VAP-B) and the late endosomeanchored protein STARD3NL. Mitochondria: brown; nucleus: blue. For further details see pp. 493-498. Image kindly provided by Fabien Alpy. - PDF Icon PDF LinkTable of Contents
Review Article|
April 11 2016
The role of phosphatidylinositol-transfer proteins at membrane contact sites
Michael Selitrennik;
Michael Selitrennik
*Molecular Cell Biology Department, Weizmann Institute of Science, Rehovot 76100, Israel
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Sima Lev
Sima Lev
1
*Molecular Cell Biology Department, Weizmann Institute of Science, Rehovot 76100, Israel
1To whom correspondence should be addressed (email Sima.Lev@weizmann.ac.il).
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Publisher: Portland Press Ltd
Received:
November 27 2015
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2016 Authors; published by Portland Press Limited
2016
Biochem Soc Trans (2016) 44 (2): 419–424.
Article history
Received:
November 27 2015
Citation
Michael Selitrennik, Sima Lev; The role of phosphatidylinositol-transfer proteins at membrane contact sites. Biochem Soc Trans 15 April 2016; 44 (2): 419–424. doi: https://doi.org/10.1042/BST20150182
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