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Sec5 concentrates at the sub-apical complex, indicating a role for Sec5 in the polarized epithelium.
Sec5 differentiates between two forms of vesicle trafficking: trafficking for cell growth and membrane protein insertion depend on sec5, whereas transmitter secretion does not
Germline clones of sec5 possess defects in membrane addition and the posterior positioning of the oocyte.
Sec5, Sec6 and Sec8 act as a complex, each member dependent on the others for proper localization and function
Rab11 forms a complex with Sec5. Sec5 interacts with Sec6 suggesting the exocyst is a Rab11 effector that facilitates protein transport to the apical rhabdomere in Drosophila photoreceptors
The Drosophila exocyst component sec5 in epithelial cells results in DE-Cad accumulation in an enlarged Rab11 recycling endosomal compartment and inhibits DE-Cad delivery to the membrane.
data suggest that the induction of SGK1 through treatment with dexamethasone alters MT dynamics to increase Sec5-GEF-H1 interactions, which promote GEF-H1 targeting to adhesion sites.
Exocyst sec5 regulates exocytosis of newcomer insulin granules underlying biphasic insulin secretion.
We identified interactions between RalA and its effectors sec5 and exo84 in the Exocyst complex as directly necessary for migration and invasion of prostate cancer tumor cells.
Data show that Mc1R, HERC2, IRF4, TYR and EXOC2 are ranked highest in hair color prediction analysis.
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.
SEC5 has been identified as a binding partner of deafness locus putative guanine nucleotide exchange factor.
evidence that mammalian exocyst components are present as distinct subcomplexes on vesicles and the plasma membrane and that Ral GTPases regulate the assembly interface of a full octameric exocyst complex through interaction with Sec5 and Exo84
These observations define the mechanistic contribution of RalGTPases to cancer cell survival and reveal the RalB/Sec5 effector complex as a component of TBK1-dependent innate immune signaling.
Localization of Exocyst and, by extension, targeting of Exocyst-dependent cargo, is dependent on Ral GTPases, which control association between Sec5 and paxillin.
Functional study of the Drosophila homolog.
the structure of the Ral-binding domain of Sec5
SEC5a copurifies in a high molecular mass fraction of 900 kD, and functions as a subunit in a exocyst complex that plays important roles in morphogenesis.
The protein encoded by this gene is a component of the exocyst complex, a multi-protein complex essential for the polarized targeting of exocytic vesicles to specific docking sites on the plasma membrane. Though best characterized in yeast, the component proteins and the functions of the exocyst complex have been demonstrated to be highly conserved in higher eukaryotes. At least eight components of the exocyst complex, including this protein, are found to interact with the actin cytoskeletal remodeling and vesicle transport machinery. This interaction has been shown to mediate filopodia formation in fibroblasts. This protein has been shown to interact with the Ral subfamily of GTPases and thereby mediate exocytosis by tethering vesicles to the plasma membrane. Alternative splicing results in multiple transcript variants.
, exocyst complex component 2
, SEC5-like 1
, exocyst complex component Sec5
, SEC5 homolog