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Exocyst complex component 4

Sec8, Sec8p, rSec8
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. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: sec6, Sec10, Sec5, Actin, Exo70
Papers using Sec8 antibodies
ARF6 controls post-endocytic recycling through its downstream exocyst complex effector
Chavrier Philippe et al., In The Journal of Cell Biology, 2000
... Anti-GM130 (clone 35) and anti–rat Sec8 (clone 14) mouse mAbs were purchased from BD Biosciences.
Characterization of a mammalian Golgi-localized protein complex, COG, that is required for normal Golgi morphology and function
Waters M. Gerard et al., In The Journal of Cell Biology, 1998
... polyclonal anti-Cog1 (anti-ldlBp) antiserum (IB, 1:3,000), affinity-purified rabbit polyclonal anti-Cog1 (anti-ldlBp) (IF, 1:150), mouse monoclonal anti-Sec8 (IB, 1:2,500; BD Biosciences), mouse monoclonal anti–β-COP (IB, ...
Papers on Sec8
RNA Silencing of Exocyst Genes in the Stigma Impairs the Acceptance of Compatible Pollen in Arabidopsis.
Goring et al., Toronto, Canada. In Plant Physiol, Dec 2015
Here, we investigated the functions of exocyst complex genes encoding the remaining seven subunits, SECRETORY3 (SEC3), SEC5, SEC6, SEC8, SEC10, SEC15, and EXO84, in Arabidopsis stigmas following compatible pollinations.
An actin filament population defined by the tropomyosin Tpm3.1 regulates glucose uptake.
Hardeman et al., Sydney, Australia. In Traffic, Jul 2015
In WAT, the amount of filamentous actin is determined by Tpm3.1 levels and is paralleled by changes in exocyst component (sec8) and Myo1c levels.
The putative exchange factor Gef3p interacts with Rho3p GTPase and the septin ring during cytokinesis in fission yeast.
Sánchez et al., Salamanca, Spain. In J Biol Chem, 2014
Although Gef3p is not essential for cell separation, the simultaneous disruption of gef3(+) and Rho3p-interacting proteins, such as Sec8p, an exocyst component, Apm1p, a subunit of the clathrin adaptor complex or For3p, an actin-polymerizing protein, yielded cells with strong defects in septation and polarity respectively.
Molecular genetic analysis of vesicular transport in Aspergillus niger reveals partial conservation of the molecular mechanism of exocytosis in fungi.
Ram et al., Leiden, Netherlands. In Microbiology, 2014
Deletion of secA, secH and ssoA (encoding SecA, SecH and SsoA the A. niger orthologues of S. cerevisiae Sec1p, Sec8p and Sso1/2p, respectively) showed that these genes are essential for A. niger, similar to the situation in S. cerevisiae.
Developmentally distinct activities of the exocyst enable rapid cell elongation and determine meristem size during primary root growth in Arabidopsis.
Fowler et al., In Bmc Plant Biol, 2013
We evaluated Arabidopsis lines with mutations in four exocyst components (SEC5, SEC8, EXO70A1 and EXO84B) to explore exocyst function in primary root growth.
Genomic analysis of Meckel-Gruber syndrome in Arabs reveals marked genetic heterogeneity and novel candidate genes.
Alkuraya et al., Riyadh, Saudi Arabia. In Eur J Hum Genet, 2013
These include C5orf42, Ellis-van-Creveld disease gene EVC2 and SEC8 (also known as EXOC4), which encodes an exocyst protein with an established role in ciliogenesis.
The exocyst complex contributes to PIN auxin efflux carrier recycling and polar auxin transport in Arabidopsis.
Zárský et al., Praha, Czech Republic. In Plant J, 2013
The recycling of PIN1 and PIN2 proteins from brefeldin-A compartments is delayed after the brefeldin-A washout in exo70A1 and sec8 exocyst mutants.
The neural cell adhesion molecule promotes FGFR-dependent phosphorylation and membrane targeting of the exocyst complex to induce exocytosis in growth cones.
Sytnyk et al., Hamburg, Germany. In J Neurosci, 2011
NCAM promotes FGF receptor-mediated phosphorylation of two tyrosine residues in the sec8 subunit of the exocyst complex and is required for efficient recruitment of the exocyst complex to growth cones.
Vesicle docking to the spindle pole body is necessary to recruit the exocyst during membrane formation in Saccharomyces cerevisiae.
Neiman et al., Stony Brook, United States. In Mol Biol Cell, 2010
Using these mpc54 mutants, we determined that recruitment of the Rab GTPase Sec4p, as well as the exocyst components Sec3p and Sec8p, to the precursor vesicles requires vesicle docking to the MOP.
Arabidopsis exocyst subunits SEC8 and EXO70A1 and exocyst interactor ROH1 are involved in the localized deposition of seed coat pectin.
Zárský et al., Praha, Czech Republic. In New Phytol, 2010
The amount of pectinaceous mucilage and seed coat structure in sec8 and exo70A1 exocyst mutants, was characterized.
The Arabidopsis exocyst complex is involved in cytokinesis and cell plate maturation.
Zársky et al., Praha, Czech Republic. In Plant Cell, 2010
During cytokinesis, green fluorescent protein-tagged exocyst subunits SEC6, SEC8, SEC15b, EXO70A1, and EXO84b exhibit distinctive localization maxima at cell plate initiation and cell plate maturation, stages with a high demand for vesicle fusion.
Different steps of sexual development are differentially regulated by the Sec8p and Exo70p exocyst subunits.
Valdivieso et al., Salamanca, Spain. In Fems Microbiol Lett, 2010
In this paper we show that in Schizosaccharomyces pombe, mating-specific cell adhesion is dependent on the exocyst subunit Sec8p, but independent of the exocyst subunit Exo70p.
Pals1 is a major regulator of the epithelial-like polarization and the extension of the myelin sheath in peripheral nerves.
Tricaud et al., Zürich, Switzerland. In J Neurosci, 2010
In addition, pals1 is required for the normal polarized localization of the vesicular markers sec8 and syntaxin4, and for the distribution of E-cadherin and myelin proteins PMP22 and MAG at the plasma membrane.
Insulin stimulates the phosphorylation of the exocyst protein Sec8 in adipocytes.
Lienhard et al., United States. In Biosci Rep, 2009
Insulin stimulates the phosphorylation of the exocyst protein Sec8 in adipocytes.
Dlg1, Sec8, and Mtmr2 regulate membrane homeostasis in Schwann cell myelination.
Bolino et al., Milano, Italy. In J Neurosci, 2009
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 interaction of IQGAP1 with the exocyst complex is required for tumor cell invasion downstream of Cdc42 and RhoA.
Chavrier et al., Paris, France. In J Cell Biol, 2008
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.
Polymorphisms near EXOC4 and LRGUK on chromosome 7q32 are associated with Type 2 Diabetes and fasting glucose; the NHLBI Family Heart Study.
Myers et al., Boston, United States. In Bmc Med Genet, 2007
EXOC4 is involved in insulin-stimulated glucose transport and may be a candidate for an association with type 2 diabetes.
Sec3p is a spatial landmark for polarized secretion in budding yeast.
Novick et al., New Haven, United States. In Cell, 1998
A functional fusion of Sec3 protein with green fluorescent protein (Sec3-GFP) localizes to the site of polarized exocytosis for each cell-cycle stage, where it colocalizes with Sec4p and Sec8p.
The cycle of SEC4 function in vesicular transport.
Bowser et al., New Haven, United States. In Ciba Found Symp, 1992
Two of these (SEC8 and SEC15) encode large proteins which form a complex that is peripherally associated with the plasma membrane.
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