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Arabidopsis group Ie formins localize to specific cell membrane domains, interact with actin-binding proteins and cause defects in cell expansion upon aberrant expression
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SYSNO ASEP 0030605 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Ostatní články Title Arabidopsis group Ie formins localize to specific cell membrane domains, interact with actin-binding proteins and cause defects in cell expansion upon aberrant expression Title Forminy skupiny Ie druhu Arabidopsis thaliana lokalizují do specifických membránových domén, interagují s aktin-vážícími bílkovinami a po aberantní expresi působí poškození buněčné expanze Author(s) Deeks, M.J. (GB)
Cvrčková, F. (CZ)
Machesky, M. L. (US)
Mikitova, V. (GB)
Ketelaar, T. (GB)
Žárský, Viktor (UEB-Q) RID, ORCID
Davies, B. (GB)
Hussey, P.J. (GB)Source Title New Phytologist - ISSN 0028-646X
Roč. 168, č. 3 (2005), s. 529-540Number of pages 12 s. Language eng - English Country CH - Switzerland Keywords actin ; Arabidopsis ; cytoskeleton Subject RIV EB - Genetics ; Molecular Biology R&D Projects GA204/02/1461 GA ČR - Czech Science Foundation (CSF) GA204/05/0268 GA ČR - Czech Science Foundation (CSF) CEZ AV0Z50380511 - UEB-Q (2005-2011) Annotation The closely related proteins AtFH4 and AtFH8 represent the group Ie clade of Arabidopsis formin homologues. The subcellular localization of these proteins and their ability to affect the actin cytoskeleton were examined. AtFH4 protein activity was identified using fluorimetric techniques. Interactions between Arabidopsis profilin isoforms and AtFH4 were assayed in vitro and in vivo using pull-down assays and yeast-2-hybrid. The subcellular localization of group Ie formins was observed with indirect immunofluorescence (AtFH4) and an ethanol-inducible green fluorescent protein (GFP) fusion construct (AtFH8). AtFH4 protein affected actin dynamics in vitro, and yeast-2-hybrid assays suggested isoform-specific interactions with the actin-binding protein profilin in vivo. Indirect immunofluorescence showed that AtFH4 localized specifically to the cell membrane at borders between adjoining cells. Expression of an AtFH8 fusion protein resulted in GFP localization to cell membrane zones, similar to AtFH4. Furthermore, aberrant expression of AtFH8 resulted in the inhibition of root hair elongation. Taken together, these data suggest that the group Ie formins act with profilin to regulate actin polymerization at specific sites associated with the cell membrane. Workplace Institute of Experimental Botany Contact David Klier, knihovna@ueb.cas.cz, Tel.: 220 390 469 Year of Publishing 2006
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