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SEC10 Sec10p

Sec10, Sec10p, hSec10
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. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Sec8, Sec5, sec6, Exo70, Actin
Papers on Sec10
Arl13b and the exocyst interact synergistically in ciliogenesis.
Barral et al., Lisbon, Portugal. In Mol Biol Cell, Feb 2016
In zebrafish, depletion of arl13b or the exocyst subunit sec10 causes phenotypes characteristic of defective cilia, such as curly tail up, edema, and abnormal pronephric kidney development.
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.
Cdc42 and sec10 Are Required for Normal Retinal Development in Zebrafish.
Lipschutz et al., Charleston, United States. In Invest Ophthalmol Vis Sci, May 2015
PURPOSE: To characterize the function and mechanisms of cdc42 and sec10 in eye development in zebrafish.
Exocyst Sec10 protects renal tubule cells from injury by EGFR/MAPK activation and effects on endocytosis.
Lipschutz et al., Taegu, South Korea. In Am J Physiol Renal Physiol, 2015
Using cell culture models, we previously demonstrated that exocyst Sec10 overexpression reduced damage to renal tubule cells and speeded recovery and that the protective effect was mediated by higher basal levels of mitogen-activated protein kinase (MAPK) signaling.
Dissecting a hidden gene duplication: the Arabidopsis thaliana SEC10 locus.
Synek et al., Praha, Czech Republic. In Plos One, 2013
Having found a surprising lack of observable phenotypic deviations and non-Mendelian segregation in Arabidopsis thaliana mutants in SEC10, a gene encoding a core subunit of the exocyst tethering complex, we examined whether this could be explained by a hidden gene duplication.
Cdc42 deficiency causes ciliary abnormalities and cystic kidneys.
Lipschutz et al., Philadelphia, United States. In J Am Soc Nephrol, 2013
In culture, the small GTPase Cdc42 co-localizes with the exocyst at primary cilia and interacts with the exocyst component Sec10.
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
At the same time, however, plasma membrane localization of GFP:EXO70A1, and the other exocyst subunits studied (GFP:SEC8 and YFP:SEC10), is resistant to brefeldin-A treatment.
The exocyst protein Sec10 interacts with Polycystin-2 and knockdown causes PKD-phenotypes.
Lipschutz et al., Philadelphia, United States. In Plos Genet, 2011
We show that knockdown of exocyst component Sec10 yields cellular phenotypes associated with ADPKD, including loss of flow-generated calcium increases, hyperproliferation, and abnormal activation of MAPK.
Exocyst Sec10 protects epithelial barrier integrity and enhances recovery following oxidative stress, by activation of the MAPK pathway.
Lipschutz et al., Philadelphia, United States. In Am J Physiol Renal Physiol, 2010
Exocyst Sec10 overexpression reduces damage to tubular epithelial barriers caused by hydrogen peroxide and speeds the recovery of normal epithelial barrier function after such an injury.
Characterization of the Arabidopsis thaliana exocyst complex gene families by phylogenetic, expression profiling, and subcellular localization studies.
Goring et al., Toronto, Canada. In New Phytol, 2010
*The exocyst is a complex of eight proteins (Sec3p, Sec5p, Sec6p, Sec8p, Sec10p, Sec15p, Exo70p and Exo84p) involved in tethering vesicles to the plasma membrane during regulated or polarized secretion.
The exocyst protein Sec10 is necessary for primary ciliogenesis and cystogenesis in vitro.
Lipschutz et al., Philadelphia, United States. In Mol Biol Cell, 2009
The exocyst protein Sec10 regulates primary ciliogenesis.
Conservation of helical bundle structure between the exocyst subunits.
Munson et al., Worcester, United States. In Plos One, 2008
We corroborate these remote homology predictions by identifying and purifying a predicted domain of yeast Sec10p, a previously insoluble exocyst subunit.
An exocyst complex functions in plant cell growth in Arabidopsis and tobacco.
Zárský et al., Praha, Czech Republic. In Plant Cell, 2008
SEC10 copurifies in a high molecular mass fraction of 900 kD, interacts with SEC15b, and functions as a subunit in a exocyst complex that plays important roles in morphogenesis.
Mammalian exocyst complex is required for the docking step of insulin vesicle exocytosis.
Rutter et al., Bristol, United Kingdom. In J Biol Chem, 2005
Overexpression of truncated, dominant-negative SEC8 or SEC10 mutants decreased the number of vesicles at the plasma membrane, whereas expression of truncated SEC6 or SEC8 inhibited overall insulin secretion.
The critical role of Exo84p in the organization and polarized localization of the exocyst complex.
Guo et al., Philadelphia, United States. In J Biol Chem, 2005
On the other hand, several exocyst members, including Sec10p, Sec15p, and Exo70p, clearly require Exo84p for their polarization.
Vesicles carry most exocyst subunits to exocytic sites marked by the remaining two subunits, Sec3p and Exo70p.
Novick et al., New Haven, United States. In J Cell Biol, 2005
One subset (Sec5p, Sec6p, Sec8p, Sec10p, Sec15p, and Exo84p) exhibits mobility similar to that of the vesicle-bound Rab family protein Sec4p, whereas Sec3p and Exo70p exhibit substantially more stability.
Involvement of the late secretory pathway in actin regulation and mRNA transport in yeast.
Gerst et al., Israel. In J Biol Chem, 2004
These included mutations in genes encoding components of the exocyst (SEC10 and SEC15), SNARE regulatory proteins (SEC1, SEC4, and SRO7), SNAREs (SEC9 and SSO1/2), and proteins involved in Golgi export (PIK1 and YPT31/32).
ARF6 controls post-endocytic recycling through its downstream exocyst complex effector.
Chavrier et al., Paris, France. In J Cell Biol, 2004
Data show that GTP-bound ARF6 interacts with Sec10, a subunit of the exocyst complex involved in docking of vesicles with the plasma membrane.
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