Abstract
It has become apparent that our textbook illustration of singular isolated organelles is obsolete. In reality, organelles form complex cooperative networks involving various types of organelles. Light microscopic and ultrastructural studies have revealed that mitochondria–endoplasmic reticulum (ER) contact sites (MERCSs) are abundant in various tissues and cell types. Indeed, MERCSs have been proposed to play critical roles in various biochemical and signaling functions such as Ca2+ homeostasis, lipid transfer, and regulation of organelle dynamics. While numerous proteins involved in these MERCS-dependent functions have been reported, how they coordinate and cooperate with each other has not yet been elucidated. In this review, we summarize the functions of mammalian proteins that localize at MERCSs and regulate their formation. We also discuss potential roles of the MERCS proteins in regulating multiple organelle contacts.
Highlights
Electron microscopy (EM) studies have revealed that a significant portion of membranes from a variety of organelles are closely apposed but do not fuse
In recent years, owing to advances in microscopy and the development of new biochemical tools, the list of proteins involved in the regulation of mitochondria–endoplasmic reticulum (ER) contact sites (MERCSs) has been dramatically expanded
Given that PDZD8 remains the only identified mammalian ortholog of the ER–mitochondria encounter structure (ERMES) core subunits (Mmm1), it is conceivable that the mammalian endoplasmic reticulum (ER) and mitochondria tethering protein complexes have not directly evolved from the yeast ERMES complex
Summary
Electron microscopy (EM) studies have revealed that a significant portion of membranes from a variety of organelles are closely apposed but do not fuse.
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