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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. (en)
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 (en)
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 (en)
skos:notation
  • RIV/00216208:11310/13:10173600!RIV14-GA0-11310___
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • I, P(GAP305/10/0433), Z(MSM0021620858)
http://linked.open...iv/cisloPeriodika
  • November
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
  • 75541
http://linked.open...ai/riv/idVysledku
  • RIV/00216208:11310/13:10173600
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • vesicle trafficking; endocytosis; cell polarity; endomembranes; plasmalemma; actin; formin (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • CH - Švýcarská konfederace
http://linked.open...ontrolniKodProRIV
  • [D9938D1C3265]
http://linked.open...i/riv/nazevZdroje
  • Frontiers in Plant 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
  • 4
http://linked.open...iv/tvurceVysledku
  • Cvrčková, Fatima
http://linked.open...n/vavai/riv/zamer
issn
  • 1664-462X
number of pages
http://bibframe.org/vocab/doi
  • 10.3389/fpls.2013.00436
http://localhost/t...ganizacniJednotka
  • 11310
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