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Sec5, Sec6 and Sec8 act as a complex, each member dependent on the others for proper localization and function
No evidence that Sec8 is required for basal neurotransmission, though glutamate receptor trafficking was mildly disrupted in sec8 mutants.
Sec8 regulates N-cadherin expression by controlling Smad3 and Smad4 expression through CBP, thereby mediating the epithelial-mesenchymal transition.
Sec8 regulate Bcl-2 and Mcl-1 expressions but not Bcl-xl in malignant peripheral nerve sheath tumor cells.
Sec8 regulates histone-modifying proteins ATF2 and RNF20.
Sec8 knockdown in HSC3 cells resulted in reduced expressions of PAK1 and PAK2 by upregulating Pirh2 and Siah1 expression, which inhibited the ERK or p38 MAPK signalling pathway and cytokeratin8 phosphorylation and cell migration.
knockdown of Sec8 enhances the binding of JIP4 to MAPK kinase 4, thereby decreasing the phosphorylation of MAPK kinase 4, JNK, and p38.
Exome sequencing revealed a likely pathogenic mutation in three novel candidate MKS disease genes-C5orf42, EVC2 and SEC8 (also known as EXOC4), which encodes an exocyst protein with an established role in ciliogenesis
High Sec8 expression is associated with progression of oral squamous-cell carcinoma by secretion of matrix metalloproteinases.
EXOC4 is involved in insulin-stimulated glucose transport and may be a candidate for an association with type 2 diabetes.
The exocyst subunits Sec3 and Sec8 interact with the polarity protein IQGAP1 and that this interaction is triggered by active Cdc42 and RhoA, which are essential for matrix degradation.
CREG1 interacts with Sec8 to promote cardiomyogenic differentiation and cell-cell adhesion.
SAP102 interacts with the PDZ-binding domain of Sec8, a member of the exocyst complex. Interactions between the two proteins are involved in the delivery of N-methyl-D-aspartate receptors to the cell surface in heterologous cells and neurons.
the exocyst complex serves to selectively regulate the docking of insulin-containing vesicles at sites of release close to the plasma membrane
Sec8 controls the directional movement of AMPA receptors towards synapses through PDZ-dependent interactions.
Insulin stimulates the phosphorylation of the exocyst protein Sec8 in adipocytes.
Interaction of Discs large 1 (Dlg1) with the Sec8 exocyst component promotes membrane addition, whereas with myotubularin-related protein 2 (Mtmr2), negatively regulates membrane formation.
The amount of pectinaceous mucilage and seed coat structure in sec8 and exo70A1 exocyst mutants, was characterized.
An allelic series of six independent T-DNA mutations reveal a role for SEC8 in male gametophyte function.
SEC8 copurifies in a high molecular mass fraction of 900 kD, interacts with SEC6, 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 multiple protein complex essential for targeting exocytic vesicles to specific docking sites on the plasma membrane. Though best characterized in yeast, the component proteins and functions of 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. The complex is also essential for the biogenesis of epithelial cell surface polarity. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
, funnel cakes
, SEC8 protein
, exocyst complex component 4
, SEC8-like 1
, exocyst complex component Sec8
, augmenter of liver regeneration (ALR) pseudogene
, secretory protein SEC8