Axonal transport of mitochondria requires milton to recruit kinesin heavy chain and is light chain independent. Kinesin mutations cause motor neuron disease phenotypes by disrupting fast axonal transport in Drosophila. Modulation of receptor recycling and degradation by the endosomal kinesin KIF16B. Role of kinesin-1 and cytoplasmic dynein in endoplasmic reticulum movement in VERO cells. Local cytoskeletal and organelle interactions impact molecular-motor-driven early endosomal trafficking. ER-associated mitochondrial division links the distribution of mitochondria and mitochondrial DNA in yeast. Mitofusin-2 independent juxtaposition of endoplasmic reticulum and mitochondria: an ultrastructural study. Identified a role for the ERMES complex in ER–mitochondria tethering in yeast.Ĭosson, P., Marchetti, A., Ravazzola, M. Performed a yeast screen for mutants that could be rescued by an artificial ER–mitochondria tether. An ER–mitochondria tethering complex revealed by a synthetic biology screen. Demonstrated that ER tubules are recruited to pre-established endosome sorting domains that undergo fission to sort cargo, and that ER dynamics are required for endosome fission. ER contact sites define the position and timing of endosome fission. Role for cER and Mmr1p in anchorage of mitochondria at sites of polarized surface growth in budding yeast. Membrane contacts between endosomes and ER provide sites for PTP1B–epidermal growth factor receptor interaction. Endoplasmic reticulum–endosome contact increases as endosomes traffic and mature. Demonstrated that ER tubules mark the site of mitochondrial division and that ER contact occurs prior to recruitment of the mammalian division machinery DRP1.įriedman, J. ER tubules mark sites of mitochondrial division. Structural and functional features and significance of the physical linkage between ER and mitochondria. Overexpression of STARD3 resulted in expansion of ER–endosome contact sites.Ĭsordás, G. Showed that the STARD3 and STARD3NL FFAT domain can interact with ER VAP proteins. Measured ER–late endosome contact site distance using electron microscopy. STARD3 or STARD3NL and VAP form a novel molecular tether between late endosomes and the ER. ![]() A 3D analysis of yeast ER structure reveals how ER domains are organized by membrane curvature. Mechanisms determining the morphology of the peripheral ER. Targeting of rough endoplasmic reticulum membrane proteins and ribosomes in invertebrate neurons. Ultra-high-resolution scanning electron microscopy of mitochondria and sarcoplasmic reticulum arrangement in human red, white, and intermediate muscle fibers. ER–organelle MCSs define the position of fission for both mitochondria and endosomes, and the ER could have a variety of roles at those specific MCSs that are destined for fission.įawcett, D. Mitochondria and endosomes undergo fission and fusion to, respectively, maintain their integrity and properly sort signalling receptors in the cell. Additionally, ER Ca 2+ release may regulate protein complexes at ER MCS. Organelles can sequester Ca 2+ released from the ER, which can regulate processes in these organelles. ER MCS may also transfer lipids between membranes.ĮR–organelle MCSs are sites of dynamic Ca 2+ crosstalk. ![]() ![]() Lipid-synthesis proteins on the ER can modify lipids on the membrane of another organelle or on protein complexes. ![]() Recently identified factors have been shown to regulate organelle trafficking through MCS formation.ĮR–organelle MCSs regulate the lipid environment of the organelle membrane apposed to the ER. Live-cell fluorescence microscopy reveals that ER-organelle MCSs can remain stable while both organelles traffic through the cell on the cytoskeleton. Ribosomes are excluded from the ER membrane at MCSs, and the distance between the ER and other membranes is close enough to suggest that the two organelles are tethered together by other proteins located on apposing membranes. The function of MCSs between the ER and mitochondria and endosomes are summarized in this Review.Įlectron microscopy studies reveal that although MCSs are less than 30 nm apart, the membranes do not fuse and each organelle maintains its identity. The endoplasmic reticulum (ER) forms tight membrane contact sites (MCSs) with several organelles in animal cells and yeast.
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