scholarly journals Myosin-dependent endoplasmic reticulum motility and F-actin organization in plant cells

2010 ◽  
Vol 107 (15) ◽  
pp. 6894-6899 ◽  
Author(s):  
H. Ueda ◽  
E. Yokota ◽  
N. Kutsuna ◽  
T. Shimada ◽  
K. Tamura ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Plant Cells ◽  
Actin Organization

Actin organization during the cell cycle in meristematic plant cells

1985 ◽  
Vol 156 (1) ◽  
pp. 231-238 ◽  
Author(s):  
Lesley Clayton ◽  
Clive W. Lloyd
Keyword(s):  
Cell Cycle ◽  
Plant Cells ◽  
Actin Organization

scholarly journals Overexpression of Arabidopsis AGD7 Causes Relocation of Golgi-Localized Proteins to the Endoplasmic Reticulum and Inhibits Protein Trafficking in Plant Cells

2007 ◽  
Vol 143 (4) ◽  
pp. 1601-1614 ◽  
Author(s):  
Myung Ki Min ◽  
Soo Jin Kim ◽  
Yansong Miao ◽  
Juyoun Shin ◽  
Liwen Jiang ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Trafficking ◽  
Plant Cells

scholarly journals Endoplasmic reticulum-localized CCX2 is required for osmotolerance by regulating ER and cytosolic Ca2+ dynamics in Arabidopsis

2018 ◽  
Vol 115 (15) ◽  
pp. 3966-3971 ◽  
Author(s):  
Massimiliano Corso ◽  
Fabrizio G. Doccula ◽  
J. Romário F. de Melo ◽  
Alex Costa ◽  
Nathalie Verbruggen
Keyword(s):  
Endoplasmic Reticulum ◽  
Osmotic Stress ◽  
Shoot Growth ◽  
Plant Cells ◽  
Loss Of Function ◽  
Adaptive Responses ◽  
Triple Mutant ◽  
Gain Of Function ◽  
Salt And Osmotic Stress ◽  
Plant Mutant

Ca2+ signals in plant cells are important for adaptive responses to environmental stresses. Here, we report that the Arabidopsis CATION/Ca2+ EXCHANGER2 (CCX2), encoding a putative cation/Ca2+ exchanger that localizes to the endoplasmic reticulum (ER), is strongly induced by salt and osmotic stresses. Compared with the WT, AtCCX2 loss-of-function mutant was less tolerant to osmotic stress and displayed the most noteworthy phenotypes (less root/shoot growth) during salt stress. Conversely, AtCCX2 gain-of-function mutants were more tolerant to osmotic stress. In addition, AtCCX2 partially suppresses the Ca2+ sensitivity of K667 yeast triple mutant, characterized by Ca2+ uptake deficiency. Remarkably, Cameleon Ca2+ sensors revealed that the absence of AtCCX2 activity results in decreased cytosolic and increased ER Ca2+ concentrations in comparison with both WT and the gain-of-function mutants. This was observed in both salt and nonsalt osmotic stress conditions. It appears that AtCCX2 is directly involved in the control of Ca2+ fluxes between the ER and the cytosol, which plays a key role in the ability of plants to cope with osmotic stresses. To our knowledge, Atccx2 is unique as a plant mutant to show a measured alteration in ER Ca2+ concentrations. In this study, we identified the ER-localized AtCCX2 as a pivotal player in the regulation of ER Ca2+ dynamics that heavily influence plant growth upon salt and osmotic stress.

Calreticulin, a multifunctional Ca2+ binding chaperone of the endoplasmic reticulum

1998 ◽  
Vol 76 (5) ◽  
pp. 779-785 ◽  
Author(s):  
Marek Michalak ◽  
Paola Mariani ◽  
Michal Opas
Keyword(s):  
Gene Expression ◽  
Endoplasmic Reticulum ◽  
Posttranslational Modification ◽  
Storage Capacity ◽  
Higher Plants ◽  
Plant Cells ◽  
Steroid Sensitive ◽  
Endoplasmic Reticulum Chaperone ◽  
Precise Role ◽  
Cellular Ca

Calreticulin is a ubiquitous endoplasmic reticulum Ca2+ binding chaperone. The protein has been implicated in a variety of diverse functions. Calreticulin is a lectin-like chaperone and, together with calnexin, it plays an important role in quality control during protein synthesis, folding, and posttranslational modification. Calreticulin binds Ca2+ and affects cellular Ca2+ homeostasis. The protein increases the Ca2+ storage capacity of the endoplasmic reticulum and modulates the function of endoplasmic reticulum Ca2+-ATPase. Calreticulin also plays a role in the control of cell adhesion and steroid-sensitive gene expression. Recently, the protein has been identified and characterized in higher plants but its precise role in plant cells awaits further investigation.Key words: calreticulin, endoplasmic reticulum, chaperone, Ca2+ binding protein.

scholarly journals Diversity and Formation of Endoplasmic Reticulum-Derived Compartments in Plants. Are These Compartments Specific to Plant Cells?: Figure 1.

2004 ◽  
Vol 136 (3) ◽  
pp. 3435-3439 ◽  
Author(s):  
Ikuko Hara-Nishimura ◽  
Ryo Matsushima ◽  
Tomoo Shimada ◽  
Mikio Nishimura
Keyword(s):  
Endoplasmic Reticulum ◽  
Plant Cells

scholarly journals Changes in the Endoplasmic Reticulum of Beetroot Slices During Aging

1967 ◽  
Vol 20 (6) ◽  
pp. 1063 ◽  
Author(s):  
Margaret E Jackman ◽  
RFM Van Steveninck
Keyword(s):  
Endoplasmic Reticulum ◽  
Plant Cells ◽  
Marked Change ◽  
Ion Accumulation ◽  
Ultrastructural Changes ◽  
Lamellar System ◽  
Cytoplasmic Vesicles

Ultrastructural changes occurring in beetroot parenchyma were studied from the time of cutting into disks and throughout the following 192 hr of aerated washing. The most marked change was the reduction of the endoplasmic reticulum to small cytoplasmic vesicles immediately after cutting (when leakage of ions is greatest), followed by a reorganization into lamellae (coinciding with the onset of net ion accumulation) and subsequent extension of the lamellar system. The possible relationships between these observations and others on plant cells are discussed.

scholarly journals Beyond Microcystins: Cyanobacterial Extracts Induce Cytoskeletal Alterations in Rice Root Cells

2020 ◽  
Author(s):  
Dimitris Pappas ◽  
Manthos Panou ◽  
Ioannis-Dimosthenis S. Adamakis ◽  
Spyros Gkelis ◽  
Emmanuel Panteris
Keyword(s):  
Plant Cells ◽  
Time Dependent ◽  
Rice Root ◽  
Enzyme Assays ◽  
Root Cells ◽  
Alpha Tubulin ◽  
Actin Organization ◽  
Seedling Roots ◽  
Time Periods ◽  
Plant Cytoskeleton

Microcystins (MCs) are cyanobacterial toxins and potent inhibitors of protein phosphatases 1 (PP1) and 2A (PP2A), which are involved in plant cytoskeleton (microtubules and F-actin) organization. Therefore, studies on the toxicity of cyanobacterial products on plant cells have so far being focused on MCs. In this study, we investigated the effects of extracts from 16 (4 MC-producing and 12 non-MC-producing) cyanobacterial strains from several habitats, on various enzymes (PP1, trypsin, elastase), on the plant cytoskeleton and H2O2 levels in Oryza sativa (rice) root cells. Seedling roots were treated for various time periods (1, 12 and 24h) with aqueous cyanobacterial extracts and underwent either immunostaining for α-tubulin or staining of F-actin with fluorescent phalloidin. DCF-DA staining was performed for H2O2 imaging. The enzyme assays confirmed the bioactivity of the extracts of not only MC-rich (MC+), but also MC-devoid (MC-) extracts, which induced major time-dependent alterations on both components of the plant cytoskeleton. These findings suggest that a broad spectrum of bioactive cyanobacterial compounds, apart from MCs or other known cyanotoxins (such as cylindrospermopsin), can affect plants by disrupting the cytoskeleton.

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