scholarly journals Expression and Ca 2+ Dependency of Plasma Membrane K + Channels of Tobacco Suspension Cells Adapted to Salt Stress

2006 ◽  
Vol 47 (12) ◽  
pp. 1674-1677 ◽  
Author(s):  
Naoki Kasukabe ◽  
Megumi Watanabe-Sugimoto ◽  
Ken Matsuoka ◽  
Eiji Okuma ◽  
Ichiro Obi ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Salt Stress ◽  
Suspension Cells ◽  
K Channels ◽  
Tobacco Suspension Cells

Extracellular Ca2+ Regulating Stomatal Movement and Plasma Membrane K+ Channels in Guard Cells of Vicia faba Under Salt Stress

2008 ◽  
Vol 34 (11) ◽  
pp. 1970-1976 ◽  
Author(s):  
Xiang ZHAO ◽  
Yan-Liang WANG ◽  
Ya-Jing WANG ◽  
Xi-Li WANG ◽  
Xiao ZHANG
Keyword(s):  
Plasma Membrane ◽  
Salt Stress ◽  
Vicia Faba ◽  
Guard Cells ◽  
Stomatal Movement ◽  
K Channels

scholarly journals Characterization of Interactions between the Soybean Salt-Stress Responsive Membrane-Intrinsic Proteins GmPIP1 and GmPIP2

Agronomy ◽  
2021 ◽  
Vol 11 (7) ◽  
pp. 1312
Author(s):  
Jia Liu ◽  
Weicong Qi ◽  
Haiying Lu ◽  
Hongbo Shao ◽  
Dayong Zhang
Keyword(s):  
Plasma Membrane ◽  
Salt Stress ◽  
Salt Tolerance ◽  
Expression Profiles ◽  
Expression Patterns ◽  
Gene Expression Profiles ◽  
Early Gene ◽  
Plant Responses ◽  
Constitutive Overexpression ◽  
Important Trait

Salt tolerance is an important trait in soybean cultivation and breeding. Plant responses to salt stress include physiological and biochemical changes that affect the movement of water across the plasma membrane. Plasma membrane intrinsic proteins (PIPs) localize to the plasma membrane and regulate the water and solutes flow. In this study, quantitative real-time PCR and yeast two-hybridization were engaged to analyze the early gene expression profiles and interactions of a set of soybean PIPs (GmPIPs) in response to salt stress. A total of 20 GmPIPs-encoding genes had varied expression profiles after salt stress. Among them, 13 genes exhibited a downregulated expression pattern, including GmPIP1;6, the constitutive overexpression of which could improve soybean salt tolerance, and its close homologs GmPIP1;7 and 1;5. Three genes showed upregulated patterns, including the GmPIP1;6 close homolog GmPIP1;4, when four genes with earlier increased and then decreased expression patterns. GmPIP1;5 and GmPIP1;6 could both physically interact strongly with GmPIP2;2, GmPIP2;4, GmPIP2;6, GmPIP2;8, GmPIP2;9, GmPIP2;11, and GmPIP2;13. Definite interactions between GmPIP1;6 and GmPIP1;7 were detected and GmPIP2;9 performed homo-interaction. The interactions of GmPIP1;5 with GmPIP2;11 and 2;13, GmPIP1;6 with GmPIP2;9, 2;11 and GmPIP2;13, and GmPIP2;9 with itself were strengthened upon salt stress rather than osmotic stress. Taken together, we inferred that GmPIP1 type and GmPIP2 type could associate with each other to synergistically function in the plant cell; a salt-stress environment could promote part of their interactions. This result provided new clues to further understand the soybean PIP–isoform interactions, which lead to potentially functional homo- and heterotetramers for salt tolerance.

scholarly journals Localization of the tight junction protein, ZO-1, is modulated by extracellular calcium and cell-cell contact in Madin-Darby canine kidney epithelial cells.

1988 ◽  
Vol 107 (6) ◽  
pp. 2389-2399 ◽  
Author(s):  
J D Siliciano ◽  
D A Goodenough
Keyword(s):  
Plasma Membrane ◽  
Extracellular Calcium ◽  
Cell Contact ◽  
Suspension Cells ◽  
Madin Darby Canine Kidney ◽  
Low Calcium ◽  
Normal Calcium ◽  
Darby Canine Kidney ◽  
Canine Kidney ◽  
Cell Cell

Using the monoclonal antibody R26.4, we have previously identified a approximately 225-kD peripheral membrane protein, named ZO-1, that is uniquely associated with the tight junction (zonula occludens) in a variety of epithelia including the Madin-Darby canine kidney (MDCK) epithelial cell line (Stevenson, B. R., J. D. Siliciano, M. S. Mooseker, and D. A. Goodenough. 1986. J. Cell Biol. 103:755-766). In this study we have analyzed the effects of cell-cell contact and extracellular calcium on the localization and the solubility of ZO-1. In confluent monolayers under normal calcium conditions, ZO-1 immunoreactivity is found exclusively at the plasma membrane in the region of the junctional complex. If MDCK cells are maintained in spinner culture under low calcium conditions, ZO-1 is diffusely organized within the cytoplasm. After the plating of suspension cells at high cell density in medium with normal calcium concentrations, ZO-1 becomes localized to the plasma membrane at sites of cell-cell contact within 5 h in a process that is independent of de novo protein synthesis. However, if suspension cells are plated at high density in low calcium medium or if suspension cells are plated at low cell density in normal calcium growth medium, ZO-1 remains diffusely organized. ZO-1 localization also becomes diffuse in monolayers that have been established in normal calcium medium and then subsequently switched into low calcium medium. These results suggest that both extracellular calcium and cell-cell contact are necessary for normal localization of ZO-1 to the plasma membrane. An analysis of the solubility properties of ZO-1 from suspension cells and monolayers revealed that high salt, nonionic detergent, and a buffer containing chelators were somewhat more effective at solubilizing ZO-1 from suspension cells than from monolayers.

scholarly journals Negative correlation between the ratio of K+to Na+and proline accumulation in tobacco suspension cells

2002 ◽  
Vol 48 (5) ◽  
pp. 753-757 ◽  
Author(s):  
Eiji Okuma ◽  
Kenji Soeda ◽  
Miho Fukuda ◽  
Mikiro Tada ◽  
Yoshiyuki Murata
Keyword(s):  
Negative Correlation ◽  
Proline Accumulation ◽  
Suspension Cells ◽  
Tobacco Suspension Cells

Heterogeneous expression of plasma-membrane-localised OsOSCA1.4 complements osmotic sensing based on hyperosmolality and salt stress in Arabidopsis osca1 mutant

Cell Calcium ◽  
2020 ◽  
Vol 91 ◽  
pp. 102261
Author(s):  
Yuanjun Zhai ◽  
Zhaohong Wen ◽  
Yang Han ◽  
Wenqing Zhuo ◽  
Fang Wang ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Salt Stress ◽  
Heterogeneous Expression

scholarly journals Regulation of callose synthase activity in situ in alamethicin-permeabilized Arabidopsis and tobacco suspension cells

2009 ◽  
Vol 9 (1) ◽  
pp. 27 ◽  
Author(s):  
Mari Aidemark ◽  
Carl-Johan Andersson ◽  
Allan G Rasmusson ◽  
Susanne Widell
Keyword(s):  
Suspension Cells ◽  
Callose Synthase ◽  
Tobacco Suspension Cells

Voltage-Dependence of Extracellular Ca2+-Induced Modification in Properties of the Inward Rectifying K+ Channels in the Plasma Membrane of Mesophyll Protoplasts of Avena sativa

1996 ◽  
Vol 23 (3) ◽  
pp. 349 ◽  
Author(s):  
J Kourie
Keyword(s):  
Plasma Membrane ◽  
Time Constant ◽  
Avena Sativa ◽  
Voltage Dependence ◽  
Membrane Current ◽  
Time Dependent ◽  
Mesophyll Cells ◽  
K Channels ◽  
Current Passing ◽  
K Current

Data obtained using the whole-celi configuration of the patch-clamp technique reveal that characteristics of the inward rectifying K+ current across the plasma membrane of protoplasts isolated from mesophyll cells of leaves of oat (Avena sativa) are modified by increasing concentrations or removing the extracellular Ca2+. The whole-cell membrane current reveals two components. The first component an initial current II* which is the sum of two currents: (a) a linear ohmic leak current passing through non-gated channels, liNGC, and (b) a rectifying inward K+ current passing through inward rectifying gated K+ channels, IKi, that are instantaneously open. The second component of the membrane current at the steady state Iss is a time-dependent K+ current IKss defined as Iss-IiNGC and passes through inward rectifying gated K+ channels. The tail K+ current, IKT, is also defined as IT-IiNGC. Raising external calcium concentration, [Ca2+]o, from 0.1 mM to 10 mM blocked the inward rectifying currents IKi, IKss and IKT. The voltage-dependence of the activation time constant (τa) for time-dependent KC current IKss was not altered significantly by increasing [Ca2+]o whereas the deactivation time constant (τd) of the IKT increased from 16 ms to 30 ms at a Vm of -100 mV. Removal of [Ca2+]o increased the amplitude and altered the characteristics of the inward rectifying K+ current. Ten minutes after the removal of [Ca2+]o the increase in IKi was 3.5-fold larger than the increase in IKss. Furthermore, removing [Ca2+]o hastened the activation of IKss and the deactivation of IKT. However, the deactivation time constant (Td) remained dependent on membrane voltage (Vm). Extracellular Ca2+ may modulate the function of mesophyll cells by regulating K+ transport through the inward rectifying K+ channels and this may have significant implications for photosynthesis and cell expansion.

Sign in / Sign up

Export Citation Format

Share Document