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Merck

Golgi-derived PI(4)P-containing vesicles drive late steps of mitochondrial division.

Science (New York, N.Y.) (2020-03-21)
Shun Nagashima, Luis-Carlos Tรกbara, Lisa Tilokani, Vincent Paupe, Hanish Anand, Joe H Pogson, Rodolfo Zunino, Heidi M McBride, Julien Prudent
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Mitochondrial plasticity is a key regulator of cell fate decisions. Mitochondrial division involves Dynamin-related protein-1 (Drp1) oligomerization, which constricts membranes at endoplasmic reticulum (ER) contact sites. The mechanisms driving the final steps of mitochondrial division are still unclear. Here, we found that microdomains of phosphatidylinositol 4-phosphate [PI(4)P] on trans-Golgi network (TGN) vesicles were recruited to mitochondria-ER contact sites and could drive mitochondrial division downstream of Drp1. The loss of the small guanosine triphosphatase ADP-ribosylation factor 1 (Arf1) or its effector, phosphatidylinositol 4-kinase IIIฮฒ [PI(4)KIIIฮฒ], in different mammalian cell lines prevented PI(4)P generation and led to a hyperfused and branched mitochondrial network marked with extended mitochondrial constriction sites. Thus, recruitment of TGN-PI(4)P-containing vesicles at mitochondria-ER contact sites may trigger final events leading to mitochondrial scission.

MATERIALS
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Sigma-Aldrich
Carbonyl cyanide 3-chlorophenylhydrazone, ≥97% (TLC), powder
Avanti
16:0-18:1 PI(4)P, Avanti Researchโ„ข - A Croda Brand 850157P, powder
Sigma-Aldrich
Monoclonal ANTI-FLAGยฎ M2 antibody produced in mouse, 1 mg/mL, clone M2, affinity isolated antibody, buffered aqueous solution (50% glycerol, 10 mM sodium phosphate, and 150 mM NaCl, pH 7.4)