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Statements

Subject Item
n2:RIV%2F00216208%3A11310%2F13%3A10173600%21RIV14-GA0-11310___
rdf:type
skos:Concept n7:Vysledek
rdfs:seeAlso
http://www.frontiersin.org/Journal/10.3389/fpls.2013.00436/full
dcterms:description
Formins are evolutionarily conserved eukaryotic proteins participating in actin and microtubule organization. Land plants have three formin clades, with only two - Class I and II - present in angiosperms. Class I formins are often transmembrane proteins, residing at the plasmalemma and anchoring the cortical cytoskeleton across the membrane to the cell wall, while Class II formins possess a PTEN-related membrane-binding domain. Lower plant Class III and non-plant formins usually contain domains predicted to bind RHO GTPases that are membrane-associated. Thus, some kind of membrane anchorage appears to be a common formin feature. Direct interactions between various non-plant formins and integral or peripheral membrane proteins have indeed been reported, with varying mechanisms and biological implications. Besides of summarizing new data on Class I and Class II formin-membrane relationships, this review surveys such %22non-classical%22 formin-membrane interactions and examines which, if any, of them may be evolutionarily conserved and operating also in plants. FYVE, SH3 and BAR domain-containing proteins emerge as possible candidates for such conserved membrane-associated formin partners. Formins are evolutionarily conserved eukaryotic proteins participating in actin and microtubule organization. Land plants have three formin clades, with only two - Class I and II - present in angiosperms. Class I formins are often transmembrane proteins, residing at the plasmalemma and anchoring the cortical cytoskeleton across the membrane to the cell wall, while Class II formins possess a PTEN-related membrane-binding domain. Lower plant Class III and non-plant formins usually contain domains predicted to bind RHO GTPases that are membrane-associated. Thus, some kind of membrane anchorage appears to be a common formin feature. Direct interactions between various non-plant formins and integral or peripheral membrane proteins have indeed been reported, with varying mechanisms and biological implications. Besides of summarizing new data on Class I and Class II formin-membrane relationships, this review surveys such %22non-classical%22 formin-membrane interactions and examines which, if any, of them may be evolutionarily conserved and operating also in plants. FYVE, SH3 and BAR domain-containing proteins emerge as possible candidates for such conserved membrane-associated formin partners.
dcterms:title
Formins and membranes: anchoring cortical actin to the cell wall and beyond Formins and membranes: anchoring cortical actin to the cell wall and beyond
skos:prefLabel
Formins and membranes: anchoring cortical actin to the cell wall and beyond Formins and membranes: anchoring cortical actin to the cell wall and beyond
skos:notation
RIV/00216208:11310/13:10173600!RIV14-GA0-11310___
n7:predkladatel
n8:orjk%3A11310
n3:aktivita
n12:Z n12:I n12:P
n3:aktivity
I, P(GAP305/10/0433), Z(MSM0021620858)
n3:cisloPeriodika
November
n3:dodaniDat
n11:2014
n3:domaciTvurceVysledku
n14:6879802
n3:druhVysledku
n20:J
n3:duvernostUdaju
n16:S
n3:entitaPredkladatele
n10:predkladatel
n3:idSjednocenehoVysledku
75541
n3:idVysledku
RIV/00216208:11310/13:10173600
n3:jazykVysledku
n22:eng
n3:klicovaSlova
vesicle trafficking; endocytosis; cell polarity; endomembranes; plasmalemma; actin; formin
n3:klicoveSlovo
n9:vesicle%20trafficking n9:cell%20polarity n9:endocytosis n9:endomembranes n9:actin n9:plasmalemma n9:formin
n3:kodStatuVydavatele
CH - Švýcarská konfederace
n3:kontrolniKodProRIV
[D9938D1C3265]
n3:nazevZdroje
Frontiers in Plant Science
n3:obor
n18:EF
n3:pocetDomacichTvurcuVysledku
1
n3:pocetTvurcuVysledku
1
n3:projekt
n13:GAP305%2F10%2F0433
n3:rokUplatneniVysledku
n11:2013
n3:svazekPeriodika
4
n3:tvurceVysledku
Cvrčková, Fatima
n3:zamer
n5:MSM0021620858
s:issn
1664-462X
s:numberOfPages
7
n17:doi
10.3389/fpls.2013.00436
n19:organizacniJednotka
11310