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Title

ORP-mediated ER contact with endocytic sites facilitates actin polymerization

AuthorsEncinar del Dedo, Javier ; Idrissi, Fátima-Zahra ; Fernández-Golbano, Isabel María ; Garcia, Patricia; Rebollo, Elena ; Krzyzanowski, Marek K.; Grötsch, Helga; Geli, María Isabel
KeywordsEndoplasmic reticulum
Endocytosis
Myosin-I
Sterol
Actin
ORP
VAP
Yeast
TREM
time-resolved electron microscopy
Issue Date4-Dec-2017
PublisherElsevier
CitationDevelopmental Cell 43(5): 588-602.e6 (2017)
AbstractOxysterol 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.
URIhttp://hdl.handle.net/10261/174523
DOIhttp://dx.doi.org/10.1016/j.devcel.2017.10.031
ISSN1534-5807
E-ISSN1878-1551
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