Molecular machineries and physiological relevance of ER-mediated membrane contacts

Membrane contact sites (MCSs) are defined as regions where two organelles are closely apposed, and most MCSs associated with each other via protein-protein or protein-lipid interactions. A number of key molecular machinery systems participate in mediating substance exchange and signal transduction,...

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Bibliographic Details
Published in:Theranostics 2021-01, Vol.11 (2), p.974-995
Main Authors: Lin, Shiyin, Meng, Tian, Huang, Haofeng, Zhuang, Haixia, He, Zhengjie, Yang, Huan, Feng, Du
Format: Article
Language:English
Subjects:
Animals
Biological Transport
Cell Membrane - metabolism
Cell Physiological Phenomena
Endoplasmic reticulum
Endoplasmic Reticulum - metabolism
Endosomes - metabolism
Humans
Intracellular Membranes - metabolism
Lipid Metabolism
Lipids
Mammals
Metabolism
Mitochondria - metabolism
Mitochondrial Membranes - metabolism
Morphology
Physiology
Proteins
Research Paper
Signal transduction
Sterols
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Summary:Membrane contact sites (MCSs) are defined as regions where two organelles are closely apposed, and most MCSs associated with each other via protein-protein or protein-lipid interactions. A number of key molecular machinery systems participate in mediating substance exchange and signal transduction, both of which are essential processes in terms of cellular physiology and pathophysiology. The endoplasmic reticulum (ER) is the largest reticulum network within the cell and has extensive communication with other cellular organelles, including the plasma membrane (PM), mitochondria, Golgi, endosomes and lipid droplets (LDs). The contacts and reactions between them are largely mediated by various protein tethers and lipids. Ions, lipids and even proteins can be transported between the ER and neighboring organelles or recruited to the contact site to exert their functions. This review focuses on the key molecules involved in the formation of different contact sites as well as their biological functions.
ISSN:1838-7640
1838-7640
DOI:10.7150/thno.51871