Journal
JOURNAL OF EXPERIMENTAL BOTANY
Volume 60, Issue 2, Pages 603-614Publisher
OXFORD UNIV PRESS
DOI: 10.1093/jxb/ern307
Keywords
Actin; actin-related protein 3 (ARP3); tobacco BY-2
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Funding
- Landesgraduierten-Programm of the State of Baden-Wurrttemberg
- Ministry of Education, Youth and Sports of the Czech Republic [LC06034]
- Baden-Wurrttemberg (LuNaCell)
- German Czech Scientific-Technical Cooperation program (WTZ)
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The polarity of actin is a central determinant of intracellular transport in plant cells. To visualize actin polarity in living plant cells, the tobacco homologue of the actin-related protein 3 (ARP3) was cloned and a fusion with the red fluorescent protein (RFP) was generated. Upon transient expression of these fusions in the tobacco cell line BY-2 (Nicotiana tabacum L. cv. Bright Yellow 2), punctate structures were observed near the nuclear envelope and in the cortical plasma. These dots could be shown to decorate actin filaments by expressing RFP-ARP3 in a marker line, where actin was tagged by GFP (green fluorescent protein)-FABD (fimbrin actin-binding domain 2). When actin filaments were disrupted by latrunculin B or by prolonged cold treatment, and subsequently allowed to recover, the actin filaments reformed from the RFP-ARP3 structures, that therefore represented actin nucleation sites. The intracellular distribution of these sites was followed during the formation of pluricellular files, and it was observed that the density of RFP-ARP3 increased in the apex of the polarized, terminal cells of a file, whereas it was equally distributed in the central cells of a file. These findings are interpreted in terms of position-dependent differences of actin organization.
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