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Review
. 2019 Apr:57:99-105.
doi: 10.1016/j.ceb.2018.12.011. Epub 2019 Feb 8.

Recent insights into mammalian ER-PM junctions

Yu-Ju Chen  1 , Carlo Giovanni Quintanilla  1 , Jen Liou  2
Affiliations
Review

Recent insights into mammalian ER-PM junctions

Yu-Ju Chen et al. Curr Opin Cell Biol. 2019 Apr.

Abstract

ER-PM junctions are subcellular sites where the endoplasmic reticulum (ER) and the plasma membrane (PM) are kept in close appositions, providing a platform for inter-organelle contact. These membrane contact sites are important for many physiological functions in mammalian cells, including excitation-contraction coupling, store-operated Ca2+ entry, and non-vesicular transfer of lipids between the ER and the PM. Here we review recent insights into the 3D structure and spatial organization of ER-PM junctions in mammalian cells as well as molecular mechanisms underlying the formation and functions of mammalian ER-PM junctions.

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Figures

Figure 1.
Figure 1.. Structure and spatial organization of ER-PM junctions.
(A) A TEM image of an ER-PM junction (red arrow head) in a MAPPER-expressing HeLa cell. (B-C) Images of the adherent surface of a MAPPER-expressing HeLa cell acquired using TIRF microscopy (TIRFM) and PALM. (D) A close-up from (C). (E) TIRF-SIM image of a HeLa cell with ER-PM junctions labeled by MAPPER (green) and stained with AF568-phalloidin for F-actin (orange). (F) A close-up from (E). (G) Diagram depicting spatial distribution of single ER-PM junctions and cortical actin. Scale bars: 1 (B), 0.2 (D), 10 (E) and 2 (F) μm. Figure 1A and 1B-F were originally published in [10] and [20].
Figure 2.
Figure 2.. Proteins enriched at mammalian ER-PM junctions.
JPH, Junctophilin; MORN, membrane occupation and recognition nexus motif; PRC, proximity restriction and clustering domain; EF-SAM, EF hand and sterile alpha motif; CC, coiled-coil domain; PB, polybasic domain; SMP, synaptotagmin-like mitochondrial-lipid binding protein domain; PITP, phosphatidylinositol transfer protein domain; FFAT, two phenylalanines (FF) in an acidic tract motif; DDHD, domain characterized by these conserved residues; LNS2, Lipin/Ned1/Smp2 domain; ORD, OSBP-related domain; PH, pleckstrin homology domain; GRAM, glucosyltransferases, Rab-like GTPase activators and myotubularins domain; ASTER, START (StAR-related lipid-transfer)-like domain.
See this image and copyright information in PMC

References

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