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ORP-Mediated ER Contact with Endocytic Sites Facilitates Actin Polymerization.

Developmental cell (2017-11-28)
Javier Encinar Del Dedo, Fatima-Zahra Idrissi, Isabel María Fernandez-Golbano, Patricia Garcia, Elena Rebollo, Marek K Krzyzanowski, Helga Grötsch, Maria Isabel Geli
RESUMEN

Oxysterol binding protein-related proteins (ORPs) are conserved lipid binding polypeptides, enriched at ER contacts sites. ORPs promote non-vesicular lipid transport and work as lipid sensors in the context of many cellular tasks, but the determinants of their distinct localization and function are not understood. Here, we demonstrate that the yeast endocytic invaginations associate with the ER and that this association specifically requires the ORPs Osh2 and Osh3, which bridge the endocytic myosin-I Myo5 to the ER integral-membrane VAMP-associated protein (VAP) Scs2. Disruption of the ER contact with endocytic sites using ORP, VAP, myosin-I, or reticulon mutants delays and weakens actin polymerization and interferes with vesicle scission. Finally, we provide evidence suggesting that ORP-dependent sterol transfer facilitates actin polymerization at endocytic sites.

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Sigma-Aldrich
Cloruro de amonio, 99.998% trace metals basis
Sigma-Aldrich
Seroalbúmina bovina, lyophilized powder, essentially IgG free, ≥96% (agarose gel electrophoresis)
Sigma-Aldrich
Peroxidase Anti-Peroxidase Soluble Complex antibody produced in rabbit, affinity isolated antibody, buffered aqueous solution