Abstract
Plant ER-PM Contact Sites in Endocytosis and Autophagy: Does the Local Composition of Membrane Phospholipid Play a Role?
Highlights
Direct interaction between the ER and PM was identified in plants in many early studies (Staehelin and Chapman, 1987; Staehelin, 1997; Perico and Sparkes, 2018), where two membranes of distinct organelles are in close apposition without fusing
The function of the plant VAP27 proteins are likely to be more diverse, and they may fulfill some of the functions of those animal EPCS proteins that are missing in plants
NET3C is a member of the NETWORKED family which is unique to plants (Deeks et al, 2012)
Summary
Direct interaction between the ER and PM was identified in plants in many early studies (Staehelin and Chapman, 1987; Staehelin, 1997; Perico and Sparkes, 2018), where two membranes of distinct organelles are in close apposition without fusing. Proteins localized to these sites have recently been identified in plants and these include VAP27, NET3C, and SYT1 (or SYTA) (Wang et al, 2014, 2016; Pérez-Sancho et al, 2015, 2016; Siao et al, 2016; McFarlane et al, 2017). Of these three proteins, VAP27 is the most well-known (as Scs in yeast and as VAP in animals). It is likely that many of the known functions of EPCS are likely to be conserved, such as the regulation of phospholipid homeostasis, endocytosis, and autophagosome formation, but the differences may reflect some plant specific additions/adaptations to their function
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