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Statements

Subject Item
n2:RIV%2F00216208%3A11310%2F12%3A10131255%21RIV13-GA0-11310___
rdf:type
skos:Concept n21:Vysledek
rdfs:seeAlso
http://www.hindawi.com/journals/scientifica/2012/712605/
dcterms:description
Formins (FH2 proteins) are an evolutionarily conserved family of eukaryotic proteins, sharing the common FH2 domain. While they have been, until recently, understood mainly as actin nucleators, formins are also engaged in various additional aspects of cytoskeletal organization and signaling, including, but not limited to, the crosstalk between the actin and microtubule networks. A surprising diversity of domain organizations has been discovered among the FH2 proteins, and specific domain setups have been found in plants. Seed plants have two clades of formins, one of them (Class I) containing mostly transmembrane proteins, while members of the other one (Class II) may be anchored to membranes via a putative membrane-binding domain related to the PTEN antioncogene. Thus, plant formins present good candidates for possible mediators of coordination of the cortical actin and microtubule cytoskeletons, as well as their attachment to the plasma membrane, that is, aspects of cell cortex organization likely to be important for cell and tissue morphogenesis. Although experimental studies of plant formin function are hampered by the large number of formin genes and their functional redundancy, recent experimental work has already resulted in some remarkable insights into the function of FH2 proteins in plants. Formins (FH2 proteins) are an evolutionarily conserved family of eukaryotic proteins, sharing the common FH2 domain. While they have been, until recently, understood mainly as actin nucleators, formins are also engaged in various additional aspects of cytoskeletal organization and signaling, including, but not limited to, the crosstalk between the actin and microtubule networks. A surprising diversity of domain organizations has been discovered among the FH2 proteins, and specific domain setups have been found in plants. Seed plants have two clades of formins, one of them (Class I) containing mostly transmembrane proteins, while members of the other one (Class II) may be anchored to membranes via a putative membrane-binding domain related to the PTEN antioncogene. Thus, plant formins present good candidates for possible mediators of coordination of the cortical actin and microtubule cytoskeletons, as well as their attachment to the plasma membrane, that is, aspects of cell cortex organization likely to be important for cell and tissue morphogenesis. Although experimental studies of plant formin function are hampered by the large number of formin genes and their functional redundancy, recent experimental work has already resulted in some remarkable insights into the function of FH2 proteins in plants.
dcterms:title
Formins: emerging players in the dynamic plant cell cortex Formins: emerging players in the dynamic plant cell cortex
skos:prefLabel
Formins: emerging players in the dynamic plant cell cortex Formins: emerging players in the dynamic plant cell cortex
skos:notation
RIV/00216208:11310/12:10131255!RIV13-GA0-11310___
n21:predkladatel
n22:orjk%3A11310
n3:aktivita
n10:Z n10:I n10:S n10:P
n3:aktivity
I, P(GAP305/10/0433), S, Z(MSM0021620858)
n3:cisloPeriodika
September 2012
n3:dodaniDat
n20:2013
n3:domaciTvurceVysledku
n7:6879802
n3:druhVysledku
n13:J
n3:duvernostUdaju
n4:S
n3:entitaPredkladatele
n8:predkladatel
n3:idSjednocenehoVysledku
137014
n3:idVysledku
RIV/00216208:11310/12:10131255
n3:jazykVysledku
n14:eng
n3:klicovaSlova
plant; cell polarity; membrane; microtubules; actin; FH2 domain; formin
n3:klicoveSlovo
n12:cell%20polarity n12:membrane n12:actin n12:FH2%20domain n12:microtubules n12:formin n12:plant
n3:kodStatuVydavatele
US - Spojené státy americké
n3:kontrolniKodProRIV
[2B8601F7BFCE]
n3:nazevZdroje
Scientifica
n3:obor
n5:EA
n3:pocetDomacichTvurcuVysledku
1
n3:pocetTvurcuVysledku
1
n3:projekt
n16:GAP305%2F10%2F0433
n3:rokUplatneniVysledku
n20:2012
n3:svazekPeriodika
2012
n3:tvurceVysledku
Cvrčková, Fatima
n3:zamer
n19:MSM0021620858
s:issn
2090-908X
s:numberOfPages
14
n18:doi
10.6064/2012/712605
n6:organizacniJednotka
11310