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Review
. 2023 Apr 18;24(8):7417.
doi: 10.3390/ijms24087417.

Signals and Their Perception for Remodelling, Adjustment and Repair of the Plant Cell Wall

Ralf Oelmüller  1 , Yu-Heng Tseng  1 , Akanksha Gandhi  1
Affiliations
Review

Signals and Their Perception for Remodelling, Adjustment and Repair of the Plant Cell Wall

Ralf Oelmüller et al. Int J Mol Sci. .

Abstract

The integrity of the cell wall is important for plant cells. Mechanical or chemical distortions, tension, pH changes in the apoplast, disturbance of the ion homeostasis, leakage of cell compounds into the apoplastic space or breakdown of cell wall polysaccharides activate cellular responses which often occur via plasma membrane-localized receptors. Breakdown products of the cell wall polysaccharides function as damage-associated molecular patterns and derive from cellulose (cello-oligomers), hemicelluloses (mainly xyloglucans and mixed-linkage glucans as well as glucuronoarabinoglucans in Poaceae) and pectins (oligogalacturonides). In addition, several types of channels participate in mechanosensing and convert physical into chemical signals. To establish a proper response, the cell has to integrate information about apoplastic alterations and disturbance of its wall with cell-internal programs which require modifications in the wall architecture due to growth, differentiation or cell division. We summarize recent progress in pattern recognition receptors for plant-derived oligosaccharides, with a focus on malectin domain-containing receptor kinases and their crosstalk with other perception systems and intracellular signaling events.

Keywords: Arabidopsis; cell wall; cell wall integrity; cellulose; hemicelluloses; malectin-domain containing proteins; pattern recognition receptors; pectin.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Phylogenetic tree of MAL- and MALL-proteins. The tree shows one branch with MAL domain (PF11721)-containing proteins (red, A) and three branches with the distantly related MALL domain (PF12819)-containing proteins (blue, B–D). For details, cf. Yang et al. [134]: (A) LRR-MAL-RLKs; (B) MALL-RLKs; (C): MALL-RLPs; (D) MALL-LRR-RLKs. Protein (and abbreviations) described in the literature are in bold (and discussed in the text). For the others, the Arabidopsis protein numbers are given. For details, cf. TAIR-homepage (arabidopsis.org).
Figure 1
Figure 1
Phylogenetic tree of MAL- and MALL-proteins. The tree shows one branch with MAL domain (PF11721)-containing proteins (red, A) and three branches with the distantly related MALL domain (PF12819)-containing proteins (blue, B–D). For details, cf. Yang et al. [134]: (A) LRR-MAL-RLKs; (B) MALL-RLKs; (C): MALL-RLPs; (D) MALL-LRR-RLKs. Protein (and abbreviations) described in the literature are in bold (and discussed in the text). For the others, the Arabidopsis protein numbers are given. For details, cf. TAIR-homepage (arabidopsis.org).
Figure 2
Figure 2
Activation, interaction and signaling of MAL- and MALL-RLKs. They are grouped according to their phylogenetic relationship (Figure 1) into LRR-MAL-RLKs, MALL-RLKs and MALL-LRR-RLKs. Arabidopsis MAL- and MALL-RLKs and GmLMM1 and LeSIRLK-like are in blue. They are activated by apoplastic microorganisms or signals (orange). Interaction partners and downstream target proteins are in green. P means phosphorylation of target proteins. Cellular responses upon activation of the RLKs are in grey boxes. Additional information, abbreviations and references are given in the text.
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