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We identified interactions between RalA (show rala Proteins) and its effectors sec5 and exo84 in the Exocyst complex as directly necessary for migration and invasion of prostate cancer tumor cells.
shRNA-mediated knockdown of the Ral effector proteins Sec5 and Exo84, but less so in the case of RalBP1, reduced oncogenic RalGEF-mediated transformation and oncogenic Ras-driven tumorigenic growth of human cells.
evidence that mammalian exocyst components are present as distinct subcomplexes on vesicles and the plasma membrane and that Ral (show rala Proteins) GTPases regulate the assembly interface of a full octameric exocyst complex through interaction with Sec5 and Exo84
Data show that TBK1 (show TBK1 Proteins) directly interacts with Exo84 through the coiled-coil domain of TBK1 (show TBK1 Proteins) and helical domain of Exo84, and knockdown of TBK1 (show TBK1 Proteins) blocked insulin (show INS Proteins)-stimulated glucose uptake and GLUT4 (show SLC2A4 Proteins) translocation.
Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
exocyst complex component 8
, exocyst complex 84-kDa subunit
, Exocyst complex component 8
, exocyst complex 84 kDa subunit
, putative protein, with a coiled coil domain, of eukaryotic origin (77.8 kD) (1P228)