gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

SEC6 Sec6p

sec6, Sec6p, rsec6
may be involved in the later stages of vesicle trafficking [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: Sec8, Sec5, ACID, Exo70, Sec10
Papers on sec6
Functional Analysis of the Exocyst Subunit Sec15 in Candida albicans.
Lee et al., Albuquerque, United States. In Eukaryot Cell, Dec 2015
In prior studies of exocyst-mediated late secretion in Candida albicans, we have determined that Sec6 contributes to cell wall integrity, secretion, and filamentation.
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.
The Candida albicans Exocyst Subunit Sec6 Contributes to Cell Wall Integrity and Is a Determinant of Hyphal Branching.
Lee et al., Albuquerque, United States. In Eukaryot Cell, Jul 2015
The yeast exocyst is a multiprotein complex comprised of eight subunits (Sec3, Sec5, Sec6, Sec8, Sec10, Sec15, Exo70, and Exo84) which orchestrates trafficking of exocytic vesicles to specific docking sites on the plasma membrane during polarized secretion.
Identification and properties of plasma membrane azole efflux pumps from the pathogenic fungi Cryptococcus gattii and Cryptococcus neoformans.
Wong et al., Ribeirão Preto, Brazil. In J Antimicrob Chemother, May 2015
Azole MICs and intracellular [(3)H]fluconazole were measured in C. gattii and C. neoformans and in S. cerevisiae expressing each cDNA of interest, as was [(3)H]fluconazole uptake by post-Golgi vesicles (PGVs) isolated from S. cerevisiae sec6-4 mutants expressing each cDNA of interest.
The contractile vacuole as a key regulator of cellular water flow in Chlamydomonas reinhardtii.
Becker et al., Köln, Germany. In Eukaryot Cell, 2014
In contrast, SEC6, a protein of the exocyst complex that is required for the water expulsion step, and a dynamin-like protein are upregulated under strong hypotonic conditions.
Regulation of cytokinesis by exocyst subunit SEC6 and KEULE in Arabidopsis thaliana.
Bao et al., Nanjing, China. In Mol Plant, 2013
In this study, using yeast two-hybrid (Y-2-H) assay, we found that SEC6 interacted with KEULE, and that a small portion of C-terminal region of KEULE was required for the interaction.
The synaptobrevin homologue Snc2p recruits the exocyst to secretory vesicles by binding to Sec6p.
Novick et al., San Diego, United States. In J Cell Biol, 2013
We observe a direct interaction between the exocyst subunit Sec6p and the latter half of the SNARE motif of Snc2p.
Visualization of the exocyst complex dynamics at the plasma membrane of Arabidopsis thaliana.
Zársky et al., Praha, Czech Republic. In Mol Biol Cell, 2013
We observed a decrease of SEC6-green fluorescent protein foci in an exo70A1 exocyst mutant.
The SEC6 protein is required for contractile vacuole function in Chlamydomonas reinhardtii.
Becker et al., Köln, Germany. In J Cell Sci, 2012
The SEC6 protein is a component of the exocyst complex that is required for efficient exocytosis.
Knockdown of Sec6 improves cell-cell adhesion by increasing α-E-catenin in oral cancer cells.
Goto et al., Yamagata, Japan. In Febs Lett, 2012
Data demonstrate that the expression of alpha-E-catenin is increased by Sec6 siRNAs, and E-cadherin and beta-catenin localize mainly at the cell-cell contact region in HSC3 cells, which were transfected with Sec6 siRNA.
Regulation of exocytosis by the exocyst subunit Sec6 and the SM protein Sec1.
Munson et al., Worcester, United States. In Mol Biol Cell, 2012
upon vesicle arrival, Sec6 is proposed to release Sec9 in favor of Sec6-exocyst assembly and to simultaneously recruit Sec1 to sites of secretion for coordinated SNARE complex formation and membrane fusion.
Selenodiglutathione uptake by the Saccharomyces cerevisiae vacuolar ATP-binding cassette transporter Ycf1p.
Blanquet et al., Palaiseau, France. In Febs J, 2011
Using secretory vesicles isolated from a sec6-4 mutant transformed either with the plasmid harbouring YCF1 or the control plasmid, we establish that the glutathione-conjugate selenodigluthatione is a high-affinity substrate of this ATP-binding cassette transporter and that oxidized glutathione is also efficiently transported.
The sterol-binding protein Kes1/Osh4p is a regulator of polarized exocytosis.
Beh et al., Canada. In Traffic, 2011
Osh4p formed complexes with the small GTPases Cdc42p, Rho1p and Sec4p, and the exocyst complex subunit Sec6p, which was also required for Osh4p association with vesicles.
Quantitative proteomics of yeast post-Golgi vesicles reveals a discriminating role for Sro7p in protein secretion.
Adler et al., Göteborg, Sweden. In Traffic, 2011
Vesicle samples isolated from PGV-accumulating sec6-4 mutants were treated with isobaric tags (iTRAQ) for subsequent quantitative tandem mass spectrometric analysis of protein content.
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.
Sec6p anchors the assembled exocyst complex at sites of secretion.
Munson et al., Worcester, United States. In Mol Biol Cell, 2009
Sec6p is required to anchor exocyst complexes at sites of secretion.
An exocyst complex functions in plant cell growth in Arabidopsis and tobacco.
Zárský et al., Praha, Czech Republic. In Plant Cell, 2008
SEC6 copurifies in a high molecular mass fraction of 900 kD, interacts with SEC8, and functions as a subunit in a exocyst complex that plays important roles in morphogenesis.
Drosophila exocyst components Sec5, Sec6, and Sec15 regulate DE-Cadherin trafficking from recycling endosomes to the plasma membrane.
Bellaïche et al., Paris, France. In Dev Cell, 2005
The Drosophila exocyst component sec6 in epithelial cells results in DE-Cad accumulation in an enlarged Rab11 recycling endosomal compartment and inhibits DE-Cad delivery to the membrane.
Targeting vesicles to specific sites on the plasma membrane: the role of the sec6/8 complex.
Scheller et al., Stanford, United States. In Trends Cell Biol, 1999
The delivery of secretory vesicles to appropriate docking and fusion sites on the plasma membrane is crucial for many cellular functions, including formation of synapses, exocytosis of neurotransmitter, establishment and maintenance of cell polarity, cell growth and plasma membrane wound healing.
Phosphatidylcholine translocase: a physiological role for the mdr2 gene.
Gros et al., Montréal, Canada. In Cell, 1994
P-glycoproteins (P-gps) encoded by the mouse mdr2 and mdr3 genes were expressed in secretory vesicles (SVs) from the yeast mutant sec6-4, and their capacity to function as a lipid translocase/flippase was tested.
share on facebooktweetadd +1mail to friends