"Cvr\u010Dkov\u00E1, Fatima" . "1664-462X" . . "Formins and membranes: anchoring cortical actin to the cell wall and beyond" . "RIV/00216208:11310/13:10173600" . . "I, P(GAP305/10/0433), Z(MSM0021620858)" . . . "[D9938D1C3265]" . . . . . "4" . . . . "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 . . . "RIV/00216208:11310/13:10173600!RIV14-GA0-11310___" . "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." . "November" . . "10.3389/fpls.2013.00436" . . . "Formins and membranes: anchoring cortical actin to the cell wall and beyond"@en . "11310" . . "1"^^ . "CH - \u0160v\u00FDcarsk\u00E1 konfederace" . "75541" . . . "vesicle trafficking; endocytosis; cell polarity; endomembranes; plasmalemma; actin; formin"@en . "Formins and membranes: anchoring cortical actin to the cell wall and beyond" . "1"^^ . "http://www.frontiersin.org/Journal/10.3389/fpls.2013.00436/full" . . . "Frontiers in Plant Science" . "Formins and membranes: anchoring cortical actin to the cell wall and beyond"@en . . . "7"^^ .