The maize actin‐depolymerizing factor, ZmADF3, redistributes to the growing tip of elongating root hairs and can be induced to translocate into the nucleus with actin

Jiang, Chang‐Jie; Weeds, Alan G.; Hussey, Patrick J.

doi:10.1046/j.1365-313x.1997.12051035.x

Cited by 112 publications

(108 citation statements)

References 33 publications

(40 reference statements)

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“…In maize roots, immunolocalization of the vegetative cellexpressed ZmADF3 showed that it redistributed from a diffuse to a tip-concentrated location as root hairs emerged and elongated (Jiang et al, 1997a). This finding is similar to observations that ADFs/cofilins localize to the leading edge of other migrating cells, where active actin remodeling is expected to occur, suggesting a probable analogous role in tip-growing root hairs.…”

Section: Introductionsupporting

confidence: 81%

The Regulation of Actin Organization by Actin-Depolymerizing Factor in Elongating Pollen Tubes[W]

et al. 2002

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Pollen tube elongation is a polarized cell growth process that transports the male gametes from the stigma to the ovary for fertilization inside the ovules. Actomyosin-driven intracellular trafficking and active actin remodeling in the apical and subapical regions of pollen tubes are both important aspects of this rapid tip growth process. Actin-depolymerizing factor (ADF) and cofilin are actin binding proteins that enhance the depolymerization of microfilaments at their minus, or slow-growing, ends. A pollen-specific ADF from tobacco, NtADF1, was used to dissect the role of ADF in pollen tube growth. Overexpression of NtADF1 resulted in the reduction of fine, axially oriented actin cables in transformed pollen tubes and in the inhibition of pollen tube growth in a dose-dependent manner. Thus, the proper regulation of actin turnover by NtADF1 is critical for pollen tube growth. When expressed at a moderate level in pollen tubes elongating in in vitro cultures, green fluorescent protein (GFP)-tagged NtADF1 (GFP-NtADF1) associated predominantly with a subapical actin mesh composed of short actin filaments and with long actin cables in the shank. Similar labeling patterns were observed for GFP-NtADF1-expressing pollen tubes elongating within the pistil. A Ser-6-to-Asp conversion abolished the interaction between NtADF1 and F-actin in elongating pollen tubes and reduced its inhibitory effect on pollen tube growth significantly, suggesting that phosphorylation at Ser-6 may be a prominent regulatory mechanism for this pollen ADF. As with some ADF/cofilin, the in vitro actin-depolymerizing activity of recombinant NtADF1 was enhanced by slightly alkaline conditions. Because a pH gradient is known to exist in the apical region of elongating pollen tubes, it seems plausible that the in vivo actin-depolymerizing activity of NtADF1, and thus its contribution to actin dynamics, may be regulated spatially by differential H ؉ concentrations in the apical region of elongating pollen tubes.

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Section: Introductionsupporting

confidence: 81%

The Regulation of Actin Organization by Actin-Depolymerizing Factor in Elongating Pollen Tubes[W]

et al. 2002

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“…In addition to the regulation of AFs in the cytoplasm, ADF is suggested to function in the nucleus as a chaperone of actin monomers (Jiang et al, 1997;Bernstein and Bamburg, 2010). Actin monomers regulate gene expression and chromatin remodeling (Zheng et al, 2009).…”

Section: Nuclear Localization and Phosphorylation Of Adf4 Are Both Immentioning

confidence: 99%

Nuclear Function of Subclass I Actin-Depolymerizing Factor Contributes to Susceptibility in Arabidopsis to an Adapted Powdery Mildew Fungus

2016

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Actin-depolymerizing factors (ADFs) are conserved proteins that function in regulating the structure and dynamics of actin microfilaments in eukaryotes. In this study, we present evidence that Arabidopsis (Arabidopsis thaliana) subclass I ADFs, particularly ADF4, functions as a susceptibility factor for an adapted powdery mildew fungus. The null mutant of ADF4 significantly increased resistance against the adapted powdery mildew fungus Golovinomyces orontii. The degree of resistance was further enhanced in transgenic plants in which the expression of all subclass I ADFs (i.e. ADF1-ADF4) was suppressed. Microscopic observations revealed that the enhanced resistance of adf4 and ADF1-4 knockdown plants (ADF1-4Ri) was associated with the accumulation of hydrogen peroxide and cell death specific to G. orontii-infected cells. The increased resistance and accumulation of hydrogen peroxide in ADF1-4Ri were suppressed by the introduction of mutations in the salicylic acid-and jasmonic acid-signaling pathways but not by a mutation in the ethylene-signaling pathway. Quantification by microscopic images detected an increase in the level of actin microfilament bundling in ADF1-4Ri but not in adf4 at early G. orontii infection time points. Interestingly, complementation analysis revealed that nuclear localization of ADF4 was crucial for susceptibility to G. orontii. Based on its G. orontii-infected-cell-specific phenotype, we suggest that subclass I ADFs are susceptibility factors that function in a direct interaction between the host plant and the powdery mildew fungus.Powdery mildew is an obligate biotrophic fungal pathogen that infects approximately 10,000 plant species, including crops, vegetables, and ornamental plants, thus causing extensive economic losses worldwide (Takamatsu, 2004). In an effort to understand the plant response to powdery mildew fungal infection and the mechanism of plant-powdery mildew fungus interactions, many mutants of host plants, particularly the model plant Arabidopsis (Arabidopsis thaliana), have been identified and analyzed.Genes for which loss causes increased resistance to a pathogen could encode factors involved in the suppression of plant immunity or susceptibility factors that function in support of the pathogenic infection. Previously identified Arabidopsis genes, the loss of whose expression causes enhanced resistance against adapted powdery mildew fungi, include POWDERY MILDEW RESISTANT1 (PMR1)

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“…The molecular link provided by the cloning of CROOKED suggests that the mechanism for actin modulation involving the ROP and BRK genes, and the ARP2/3 complex may be well conserved between plants and other organisms. The complex is also known to interact with profilins (Mullins et al, 1998b), actindepolymerizing-factors (ADF/cofilin) (Svitkina and Borisy, 1999), which along with different F-actin bundling proteins are already known to share the same intracellular domains in expanding plant cells (Jiang et al, 1997;Dong et al, 2001;Vidali et al, 2001;Vantard and Blanchoin, 2002). Finally, although not addressed here, the crooked mutant provides an enviable tool to understand the interactions between the actin and microtubular components of the cytoskeleton in higher plants, including their apparent cooperative roles in subcellular motility and cell morphogenesis.…”

Section: The Molecular Identification Of Crooked Links Different Regumentioning

confidence: 99%

Arabidopsis CROOKEDencodes for the smallest subunit of the ARP2/3 complex and controls cell shape by region specific fine F-actin formation

et al. 2003

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The generation of a specific cell shape requires differential growth, whereby specific regions of the cell expand more relative to others. The Arabidopsis crooked mutant exhibits aberrant cell shapes that develop because of mis-directed expansion, especially during a rapid growth phase. GFPaided visualization of the F-actin cytoskeleton and the behavior of subcellular organelles in different cell-types in crooked and wild-type Arabidopsis revealed that localized expansion is promoted in cellular regions with fine F-actin arrays but is restricted in areas that maintain dense Factin. This suggested that a spatiotemporal distinction between fine versus dense F-actin in a growing cell could determine the final shape of the cell. CROOKED was molecularly identified as the plant homolog of ARPC5, the smallest sub-unit of the ARP2/3 complex that in other organisms is renowned for its role in creating dendritic arrays of fine F-actin. Rescue of crooked phenotype by the human ortholog provides the first molecular evidence for the presence and functional conservation of the complex in higher plants. Our cell-biological and molecular characterization of CROOKED suggests a general actinbased mechanism for regulating differential growth and generating cell shape diversity.

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The maize actin‐depolymerizing factor, ZmADF3, redistributes to the growing tip of elongating root hairs and can be induced to translocate into the nucleus with actin

Cited by 112 publications

References 33 publications

The Regulation of Actin Organization by Actin-Depolymerizing Factor in Elongating Pollen Tubes[W]

The Regulation of Actin Organization by Actin-Depolymerizing Factor in Elongating Pollen Tubes[W]

Nuclear Function of Subclass I Actin-Depolymerizing Factor Contributes to Susceptibility in Arabidopsis to an Adapted Powdery Mildew Fungus

Arabidopsis CROOKEDencodes for the smallest subunit of the ARP2/3 complex and controls cell shape by region specific fine F-actin formation

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