Rice Morphology Determinant-Mediated Actin Filament Organization Contributes to Pollen Tube Growth

Li, Gang; Yang, Xiujuan; Zhang, Xiaoqing; Yu, Shanlin; Liang, Wanqi; Zhang, Dabing

doi:10.1104/pp.17.01759

Cited by 23 publications

(19 citation statements)

References 68 publications

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“…RMD binds to actin filaments (AFs) in vitro and affects actin organization in roots and pollen tubes (Yang et al, 2011;Zhang et al, 2011;Li et al, 2018). To first assess whether the actin cytoskeleton is important for shoot gravitropism, we transferred germinated wild-type rice seeds to half-strength Murashige and Skoog (MS) liquid medium supplemented with 1 mM of LatB, an actin polymerization inhibitor (Baluška et al, 2001).…”

Section: Organization Of the Actin Cytoskeleton Is Disturbed In The Smentioning

confidence: 99%

“…Previously, we showed that the actin cytoskeleton in rice (Oryza sativa) is controlled by Rice Morphology Determinant (RMD, also called "BUI1"), a type-II formin protein specifying rice morphology by regulating actin nucleation and organization . RMD also regulates actin dynamics and auxin homeostasis during root cell elongation and growth (Li et al, 2014), as well as pollen tube development (Li et al, 2018), and it is required for crown root angle in response to P starvation . Here, we show that RMD promotes shoot negative gravitropism by regulating actin organization and amyloplast sedimentation in the endodermis of light-grown shoots.…”

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confidence: 99%

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The Rice Actin-Binding Protein RMD Regulates Light-Dependent Shoot Gravitropism

Nowak

et al. 2019

Plant Physiol.

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Light and gravity are two key determinants in orientating plant stems for proper growth and development. The organization and dynamics of the actin cytoskeleton are essential for cell biology and critically regulated by actin-binding proteins. However, the role of actin cytoskeleton in shoot negative gravitropism remains controversial. In this work, we report that the actin-binding protein Rice Morphology Determinant (RMD) promotes reorganization of the actin cytoskeleton in rice (Oryza sativa) shoots. The changes in actin organization are associated with the ability of the rice shoots to respond to negative gravitropism. Here, lightgrown rmd mutant shoots exhibited agravitropic phenotypes. By contrast, etiolated rmd shoots displayed normal negative shoot gravitropism. Furthermore, we show that RMD maintains an actin configuration that promotes statolith mobility in gravisensing endodermal cells, and for proper auxin distribution in light-grown, but not dark-grown, shoots. RMD gene expression is diurnally controlled and directly repressed by the phytochrome-interacting factor-like protein OsPIL16. Consequently, overexpression of OsPIL16 led to gravisensing and actin patterning defects that phenocopied the rmd mutant. Our findings outline a mechanism that links light signaling and gravity perception for straight shoot growth in rice.

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Section: Organization Of the Actin Cytoskeleton Is Disturbed In The Smentioning

confidence: 99%

mentioning

confidence: 99%

The Rice Actin-Binding Protein RMD Regulates Light-Dependent Shoot Gravitropism

Nowak

et al. 2019

Plant Physiol.

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“…This has later been confirmed in the case of the Physcomitrella patens For2A formin whose PTEN-like domain interacts with PI(3,5)P 2 ; this interaction is necessary for formin localization to the tip of apically growing cells [19]. Similarly, the PTEN-like domain of the rice Class II formin FH5 encoded by rice morphology determinant (RMD) gene determines tip localization of this protein in pollen tubes [20] and interestingly also mediates its anchorage to the outer surface of chloroplasts [21]. In Arabidopsis, the only typical Class II formin containing a PTEN-like domain experimentally characterized so far is AtFH14 (At1g31810), whose dimer can bind to actin barbed ends [22] and which associates with microtubules in mitotic BY-2 cells, participating in the control of mitosis and cytokinesis [23].…”

Section: Introductionmentioning

confidence: 79%

“…This suggests that integrity of microtubules is essential to maintain subcellular distribution of AtFH13. Since both AtFH13 and AtFH14 contain the PTEN-like domain known to associate with membranes [20,24], we hypothesized that the fluorescent cytoplasmic punctate structures not associated with the cytoskeleton may be related to compartments of the endomembrane system. We thus examined co-localization of AtFH13-YFP and AtFH14-YFP with the ER marker ER-rk (ER red kanamycin).…”

Section: Int J Mol Sci 2020 20 X For Peer Review 4 Of 16mentioning

confidence: 99%

Arabidopsis Class II Formins AtFH13 and AtFH14 Can Form Heterodimers but Exhibit Distinct Patterns of Cellular Localization

Kollárová

Forero

Stillerová

et al. 2020

IJMS

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Formins are evolutionarily conserved multi-domain proteins participating in the control of both actin and microtubule dynamics. Angiosperm formins form two evolutionarily distinct families, Class I and Class II, with class-specific domain layouts. The model plant Arabidopsis thaliana has 21 formin-encoding loci, including 10 Class II members. In this study, we analyze the subcellular localization of two A. thaliana Class II formins exhibiting typical domain organization, the so far uncharacterized formin AtFH13 (At5g58160) and its distant homolog AtFH14 (At1g31810), previously reported to bind microtubules. Fluorescent protein-tagged full length formins and their individual domains were transiently expressed in Nicotiana benthamiana leaves under the control of a constitutive promoter and their subcellular localization (including co-localization with cytoskeletal structures and the endoplasmic reticulum) was examined using confocal microscopy. While the two formins exhibit distinct and only partially overlapping localization patterns, they both associate with microtubules via the conserved formin homology 2 (FH2) domain and with the periphery of the endoplasmic reticulum, at least in part via the N-terminal PTEN (Phosphatase and Tensin)-like domain. Surprisingly, FH2 domains of AtFH13 and AtFH14 can form heterodimers in the yeast two-hybrid assay—a first case of potentially biologically relevant formin heterodimerization mediated solely by the FH2 domain.

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“…On the other hand, and plant growth has not been clarified yet. Recently, Li et al, (2018) reported that elongation growth of rice pollen tube was suppressed, when the density of actin filaments was decreased. Thus, regulation of the density of actin filaments may be involved in the modification of growth anisotropy by hypergravity in azuki bean epicotyls.…”

Section: Resultsmentioning

confidence: 99%

Dynamics of Actin Filaments in Epidermal Cells of Azuki Bean Epicotyls under Hypergravity Conditions

et al. 2018

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The effects of hypergravity on growth and dynamics of actin filaments were examined in azuki bean (Vigna angularis) epicotyls. Elongation growth occurred mainly in the apical region of epicotyls, which was inhibited by hypergravity at 300 G. The density of actin filaments in epidermal cells decreased from the apical to the basal regions of epicotyls, irrespective of the gravitational conditions, and in the apical region of epicotyls, hypergravity decreased the density. Actin filaments were arranged with longitudinal or radial direction in the epidermal cells of apical region of 1 G-grown epicotyls. On the other hand, actin filaments with transverse direction were observed in basal region of epicotyls grown at 1 G. Similar changes in the arrangement of actin filaments toward the basal region were observed even under hypergravity conditions. Hypergravity had no effects on the growth and reorientation of cortical microtubules, when actin filaments were disrupted by cytochalasin D treatment. These results suggest that modification of dynamics of actin filaments is responsible for reorientation of cortical microtubules, which leads to inhibition of elongation growth in azuki bean epicotyls under hypergravity conditions

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Rice Morphology Determinant-Mediated Actin Filament Organization Contributes to Pollen Tube Growth

Cited by 23 publications

References 68 publications

The Rice Actin-Binding Protein RMD Regulates Light-Dependent Shoot Gravitropism

The Rice Actin-Binding Protein RMD Regulates Light-Dependent Shoot Gravitropism

Arabidopsis Class II Formins AtFH13 and AtFH14 Can Form Heterodimers but Exhibit Distinct Patterns of Cellular Localization

Dynamics of Actin Filaments in Epidermal Cells of Azuki Bean Epicotyls under Hypergravity Conditions

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