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Sec5, Sec6 (show EXOC3 Proteins) 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 (show GRIN2A Proteins) receptor trafficking was mildly disrupted in sec8 mutants.
Sec8 regulates N-cadherin (show CDH2 Proteins) expression by controlling Smad3 (show SMAD3 Proteins) and Smad4 (show SMAD4 Proteins) expression through CBP (show CREBBP Proteins), thereby mediating the epithelial-mesenchymal transition.
Sec8 regulate Bcl-2 (show BCL2 Proteins) and Mcl-1 (show MCL1 Proteins) expressions but not Bcl-xl (show BCL2L1 Proteins) in malignant peripheral nerve sheath tumor cells.
Sec8 regulates histone-modifying proteins ATF2 (show ATF2 Proteins) and RNF20 (show RNF20 Proteins).
Sec8 knockdown in HSC3 cells resulted in reduced expressions of PAK1 (show PAK1 Proteins) and PAK2 (show PAK2 Proteins) by upregulating Pirh2 (show RCHY1 Proteins) and Siah1 (show SIAH1 Proteins) expression, which inhibited the ERK (show EPHB2 Proteins) or p38 MAPK (show MAPK14 Proteins) signalling pathway and cytokeratin8 phosphorylation and cell migration.
knockdown of Sec8 enhances the binding of JIP4 (show SPAG9 Proteins) to MAPK (show MAPK1 Proteins) kinase 4, thereby decreasing the phosphorylation of MAPK (show MAPK1 Proteins) kinase 4, JNK (show MAPK8 Proteins), and p38 (show CRK Proteins).
Exome sequencing revealed a likely pathogenic mutation in three novel candidate MKS (show MKS1 Proteins) disease genes-C5orf42, EVC2 (show EVC2 Proteins) 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 (show INS Proteins)-stimulated glucose transport and may be a candidate for an association with type 2 diabetes.
The exocyst subunits Sec3 (show EXOC1 Proteins) and Sec8 interact with the polarity protein IQGAP1 (show IQGAP1 Proteins) and that this interaction is triggered by active Cdc42 (show CDC42 Proteins) and RhoA (show RHOA Proteins), which are essential for matrix degradation.
CREG1 (show CREG1 Proteins) interacts with Sec8 to promote cardiomyogenic differentiation and cell-cell adhesion.
SAP102 (show DLG3 Proteins) 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 (show INS Proteins)-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 (show INS Proteins) stimulates the phosphorylation of the exocyst protein Sec8 in adipocytes.
Interaction of Discs large 1 (Dlg1 (show DLG4 Proteins)) with the Sec8 exocyst component promotes membrane addition, whereas with myotubularin-related protein 2 (Mtmr2 (show MTMR2 Proteins)), 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 (show EXOC3 Proteins), 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