This HTML5 document contains 59 embedded RDF statements represented using HTML+Microdata notation.

The embedded RDF content will be recognized by any processor of HTML5 Microdata.

Namespace Prefixes

PrefixIRI
dctermshttp://purl.org/dc/terms/
n8http://localhost/temp/predkladatel/
n19http://linked.opendata.cz/resource/domain/vavai/projekt/
n17http://linked.opendata.cz/resource/domain/vavai/riv/tvurce/
n11http://linked.opendata.cz/resource/domain/vavai/subjekt/
n10http://linked.opendata.cz/ontology/domain/vavai/
n15http://linked.opendata.cz/resource/domain/vavai/vysledek/RIV%2F00216208%3A11310%2F13%3A10190704%21RIV14-GA0-11310___/
n13http://linked.opendata.cz/resource/domain/vavai/zamer/
shttp://schema.org/
skoshttp://www.w3.org/2004/02/skos/core#
rdfshttp://www.w3.org/2000/01/rdf-schema#
n3http://linked.opendata.cz/ontology/domain/vavai/riv/
n16http://bibframe.org/vocab/
n2http://linked.opendata.cz/resource/domain/vavai/vysledek/
rdfhttp://www.w3.org/1999/02/22-rdf-syntax-ns#
n7http://linked.opendata.cz/ontology/domain/vavai/riv/klicoveSlovo/
n4http://linked.opendata.cz/ontology/domain/vavai/riv/duvernostUdaju/
xsdhhttp://www.w3.org/2001/XMLSchema#
n18http://linked.opendata.cz/ontology/domain/vavai/riv/jazykVysledku/
n12http://linked.opendata.cz/ontology/domain/vavai/riv/aktivita/
n21http://linked.opendata.cz/ontology/domain/vavai/riv/druhVysledku/
n14http://linked.opendata.cz/ontology/domain/vavai/riv/obor/
n20http://reference.data.gov.uk/id/gregorian-year/

Statements

Subject Item
n2:RIV%2F00216208%3A11310%2F13%3A10190704%21RIV14-GA0-11310___
rdf:type
n10:Vysledek skos:Concept
rdfs:seeAlso
http://dx.doi.org/10.1091/mbc.E12-06-0492
dcterms:description
The exocyst complex, an effector of Rho and Rab GTPases, is believed to function as an exocytotic vesicle tether at the plasma membrane before soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex formation. Exocyst subunits localize to secretory-active regions of the plasma membrane, exemplified by the outer domain of Arabidopsis root epidermal cells. Using variable-angle epifluorescence microscopy, we visualized the dynamics of exocyst subunits at this domain. The subunits colocalized in defined foci at the plasma membrane, distinct from endocytic sites. Exocyst foci were independent of cytoskeleton, although prolonged actin disruption led to changes in exocyst localization. Exocyst foci partially overlapped with vesicles visualized by VAMP721 v-SNARE, but the majority of the foci represent sites without vesicles, as indicated by electron microscopy and drug treatments, supporting the concept of the exocyst functioning as a dynamic particle. We observed a decrease of SEC6-green fluorescent protein foci in an exo70A1 exocyst mutant. Finally, we documented decreased VAMP721 trafficking to the plasma membrane in exo70A1 and exo84b mutants. Our data support the concept that the exocyst-complex subunits dynamically dock and undock at the plasma membrane to create sites primed for vesicle tethering. The exocyst complex, an effector of Rho and Rab GTPases, is believed to function as an exocytotic vesicle tether at the plasma membrane before soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex formation. Exocyst subunits localize to secretory-active regions of the plasma membrane, exemplified by the outer domain of Arabidopsis root epidermal cells. Using variable-angle epifluorescence microscopy, we visualized the dynamics of exocyst subunits at this domain. The subunits colocalized in defined foci at the plasma membrane, distinct from endocytic sites. Exocyst foci were independent of cytoskeleton, although prolonged actin disruption led to changes in exocyst localization. Exocyst foci partially overlapped with vesicles visualized by VAMP721 v-SNARE, but the majority of the foci represent sites without vesicles, as indicated by electron microscopy and drug treatments, supporting the concept of the exocyst functioning as a dynamic particle. We observed a decrease of SEC6-green fluorescent protein foci in an exo70A1 exocyst mutant. Finally, we documented decreased VAMP721 trafficking to the plasma membrane in exo70A1 and exo84b mutants. Our data support the concept that the exocyst-complex subunits dynamically dock and undock at the plasma membrane to create sites primed for vesicle tethering.
dcterms:title
Visualization of the exocyst complex dynamics at the plasma membrane of Arabidopsis thaliana Visualization of the exocyst complex dynamics at the plasma membrane of Arabidopsis thaliana
skos:prefLabel
Visualization of the exocyst complex dynamics at the plasma membrane of Arabidopsis thaliana Visualization of the exocyst complex dynamics at the plasma membrane of Arabidopsis thaliana
skos:notation
RIV/00216208:11310/13:10190704!RIV14-GA0-11310___
n10:predkladatel
n11:orjk%3A11310
n3:aktivita
n12:Z n12:P n12:I
n3:aktivity
I, P(GAP305/11/1629), Z(AV0Z50380511)
n3:cisloPeriodika
4
n3:dodaniDat
n20:2014
n3:domaciTvurceVysledku
n17:9081186 n17:5470056
n3:druhVysledku
n21:J
n3:duvernostUdaju
n4:S
n3:entitaPredkladatele
n15:predkladatel
n3:idSjednocenehoVysledku
114217
n3:idVysledku
RIV/00216208:11310/13:10190704
n3:jazykVysledku
n18:eng
n3:klicovaSlova
endocytosis; golgi; sites; vesicle; exocytosis; live cells; cell polarity; mammalian exocyst; polarized secretion; plant transformation
n3:klicoveSlovo
n7:exocytosis n7:polarized%20secretion n7:cell%20polarity n7:golgi n7:mammalian%20exocyst n7:endocytosis n7:sites n7:vesicle n7:plant%20transformation n7:live%20cells
n3:kodStatuVydavatele
GB - Spojené království Velké Británie a Severního Irska
n3:kontrolniKodProRIV
[1A9157CBA002]
n3:nazevZdroje
Molecular Biology of the Cell
n3:obor
n14:ED
n3:pocetDomacichTvurcuVysledku
2
n3:pocetTvurcuVysledku
8
n3:projekt
n19:GAP305%2F11%2F1629
n3:rokUplatneniVysledku
n20:2013
n3:svazekPeriodika
24
n3:tvurceVysledku
de Rycke, Riet Nowack, Moritz K. Synek, Lukas Fendrych, Matyas Žárský, Viktor Pečenková, Tamara Sekereš, Juraj Drdova, Edita Jankova
n3:wos
000321117800008
n3:zamer
n13:AV0Z50380511
s:issn
1059-1524
s:numberOfPages
11
n16:doi
10.1091/mbc.E12-06-0492
n8:organizacniJednotka
11310