scholarly journals Cell wall contributes to the stability of plasma membrane nanodomain organization of Arabidopsis thaliana FLOTILLIN2 and HYPERSENSITIVE INDUCED REACTION1 proteins

2019 ◽  
Vol 101 (3) ◽  
pp. 619-636 ◽  
Author(s):  
Michal Daněk ◽  
Jindřiška Angelini ◽  
Kateřina Malínská ◽  
Jan Andrejch ◽  
Zuzana Amlerová ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Cell Wall ◽  
Plasma Membrane ◽  
The Stability

scholarly journals AT14A mediates the cell wall-plasma membrane-cytoskeleton continuum in Arabidopsis thaliana cells

2012 ◽  
Vol 63 (11) ◽  
pp. 4061-4069 ◽  
Author(s):  
B. Lu ◽  
J. Wang ◽  
Y. Zhang ◽  
H. Wang ◽  
J. Liang ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Cell Wall ◽  
Plasma Membrane ◽  
Membrane Cytoskeleton

scholarly journals LRR-extensins of vegetative tissues are a functionally conserved family of RALF1 receptors interacting with the receptor kinase FERONIA

2019 ◽  
Author(s):  
Aline Herger ◽  
Shibu Gupta ◽  
Gabor Kadler ◽  
Christina Maria Franck ◽  
Aurélien Boisson-Dernier ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Cell Wall ◽  
Plasma Membrane ◽  
Cell Growth ◽  
Mechanical Stability ◽  
Root Hairs ◽  
Cell Wall Integrity ◽  
Receptor Kinase ◽  
Growth Processes ◽  
Evolutionary Diversification

AbstractPlant cell growth requires the coordinated expansion of the protoplast and the cell wall that confers mechanical stability to the cell. An elaborate system of cell wall integrity sensors monitors cell wall structures and conveys information on cell wall composition and growth factors to the cell. LRR-extensins (LRXs) are cell wall-attached extracellular regulators of cell wall formation and high-affinity binding sites for RALF (rapid alkalinization factor) peptide hormones that trigger diverse physiological processes related to cell growth. RALF peptides are also perceived by receptors at the plasma membrane and LRX4 of Arabidopsis thaliana has been shown to also interact with one of these receptors, FERONIA (FER). Here, we demonstrate that several LRXs, including the main LRX protein of root hairs, LRX1, interact with FER and RALF1 to coordinate growth processes. Membrane association of LRXs correlate with binding to FER, indicating that LRXs represent a physical link between intra- and extracellular compartments via interaction with membrane-localized proteins. Finally, despite evolutionary diversification of the LRR domains of various LRX proteins, many of them are functionally still overlapping, indicative of LRX proteins being central players in regulatory processes that are conserved in very different cell types.Author SummaryCell growth in plants requires the coordinated enlargement of the cell and the surrounding cell wall, which is ascertained by an elaborate system of cell wall integrity sensors, proteins involved in the exchange of information between the cell and the cell wall. In Arabidopsis thaliana, LRR-extensins (LRXs) are localized in the cell wall and are binding RALF peptides, hormones that regulate cell growth-related processes. LRX4 also binds the plasma membrane-localized receptor kinase FERONIA (FER), establishing a link between the cell and the cell wall. It is not clear, however, whether the different LRXs of Arabidopsis have similar functions and how they interact with their binding partners. Here, we demonstrate that interaction with FER and RALFs requires the LRR domain of LRXs and several but not all LRXs can bind these proteins. This explains the observation that mutations in several of the LRXs induce phenotypes comparable to a fer mutant, establishing that LRX-FER interaction is important for proper cell growth. Some LRXs, however, appear to influence cell growth processes in different ways, which remain to be identified.

High affinity RGD-binding sites at the plasma membrane of Arabidopsis thaliana links the cell wall

1998 ◽  
Vol 16 (1) ◽  
pp. 63-71 ◽  
Author(s):  
Herve Canut ◽  
Antoine Carrasco ◽  
Jean-Philippe Galaud ◽  
Catherine Cassan ◽  
Huguette Bouyssou ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Cell Wall ◽  
Plasma Membrane ◽  
Binding Sites ◽  
High Affinity

Microanatomy of the Periplasm of Bacillus Licheniformis

1971 ◽  
Vol 29 ◽  
pp. 262-263
Author(s):  
B.K. Ghosh
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Bacillus Licheniformis ◽  
External Environment ◽  
Permeability Barrier ◽  
Periplasmic Space ◽  
Modified Technique ◽  
Gram Positive ◽  
Gram Negative ◽  
Gram Positive Bacteria

Periplasm of bacteria is the space outside the permeability barrier of plasma membrane but enclosed by the cell wall. The contents of this special milieu exterior could be regulated by the plasma membrane from the internal, and by the cell wall from the external environment of the cell. Unlike the gram-negative organism, the presence of this space in gram-positive bacteria is still controversial because it cannot be clearly demonstrated. We have shown the importance of some periplasmic bodies in the secretion of penicillinase from Bacillus licheniformis.In negatively stained specimens prepared by a modified technique (Figs. 1 and 2), periplasmic space (PS) contained two kinds of structures: (i) fibrils (F, 100 Å) running perpendicular to the cell wall from the protoplast and (ii) an array of vesicles of various sizes (V), which seem to have evaginated from the protoplast.

Enrichment of vitronectin- and fibronectin-like proteins in NaCI-adapted plant cells and evidence for their involvement in plasma membrane-cell wall adhesion

1993 ◽  
Vol 3 (5) ◽  
pp. 637-646 ◽  
Author(s):  
Jian-Kang Zhu ◽  
Jun Shi ◽  
Utpal Singh ◽  
Sarah E. Wyatt ◽  
Ray A. Bressan ◽  
...  
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Plant Cells ◽  
Membrane Cell
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