About: The plant formin AtFH4 interacts with both actin and microtubules, and contains a newly identified microtubule-binding domain     Goto   Sponge   NotDistinct   Permalink

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Description
  • The dynamic behaviour of the actin cytoskeleton in plants relies on the coordinated action of several classes of actin-binding proteins (ABPs). These ABPs include the plant-specific subfamilies of actin-nucleating formin proteins. The model plant species Arabidopsis thaliana has over 20 formin proteins, all of which contain plant-specific regions in place of the GTPase-binding domain, formin homology (FH)3 domain, and DAD and DID motifs found in many fungal and animal formins. We have identified for the first time a plant-specific region of the membrane-integrated formin AtFH4 that mediates an association with the microtubule cytoskeleton. In vitro analysis shows that this region (named the GOE domain) binds directly to microtubules. Overexpressed AtFH4 accumulates at the endoplasmic reticulum membrane and co-aligns the endoplasmic reticulum with microtubules. The FH1 and FH2 domains of formins are conserved in plants, and we show that these domains of AtFH4 nucleate F-actin.
  • The dynamic behaviour of the actin cytoskeleton in plants relies on the coordinated action of several classes of actin-binding proteins (ABPs). These ABPs include the plant-specific subfamilies of actin-nucleating formin proteins. The model plant species Arabidopsis thaliana has over 20 formin proteins, all of which contain plant-specific regions in place of the GTPase-binding domain, formin homology (FH)3 domain, and DAD and DID motifs found in many fungal and animal formins. We have identified for the first time a plant-specific region of the membrane-integrated formin AtFH4 that mediates an association with the microtubule cytoskeleton. In vitro analysis shows that this region (named the GOE domain) binds directly to microtubules. Overexpressed AtFH4 accumulates at the endoplasmic reticulum membrane and co-aligns the endoplasmic reticulum with microtubules. The FH1 and FH2 domains of formins are conserved in plants, and we show that these domains of AtFH4 nucleate F-actin. (en)
Title
  • The plant formin AtFH4 interacts with both actin and microtubules, and contains a newly identified microtubule-binding domain
  • The plant formin AtFH4 interacts with both actin and microtubules, and contains a newly identified microtubule-binding domain (en)
skos:prefLabel
  • The plant formin AtFH4 interacts with both actin and microtubules, and contains a newly identified microtubule-binding domain
  • The plant formin AtFH4 interacts with both actin and microtubules, and contains a newly identified microtubule-binding domain (en)
skos:notation
  • RIV/61389030:_____/10:00350394!RIV11-GA0-61389030
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(GAP305/10/0433), P(LC06004), S, Z(AV0Z50380511), Z(MSM0021620858)
http://linked.open...iv/cisloPeriodika
  • 8
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 279084
http://linked.open...ai/riv/idVysledku
  • RIV/61389030:_____/10:00350394
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • Actin regulating proteins; Membrane; Microtubule (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • GB - Spojené království Velké Británie a Severního Irska
http://linked.open...ontrolniKodProRIV
  • [AEF29975E6AC]
http://linked.open...i/riv/nazevZdroje
  • Journal of Cell Science
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 123
http://linked.open...iv/tvurceVysledku
  • Žárský, Viktor
  • Fendrych, Matyáš
  • Cvrčková, F.
  • Bell, K. S.
  • Deeks, M. J.
  • Hussey, P. J.
  • Oparka, K.
  • Smertenko, A.
http://linked.open...ain/vavai/riv/wos
  • 000276568200004
http://linked.open...n/vavai/riv/zamer
issn
  • 0021-9533
number of pages
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