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Overlapping functions and protein-protein interactions of LRR-extensins in Arabidopsis

Plant cell growth requires the coordinated expansion of the protoplast and the cell wall, which is controlled by an elaborate system of cell wall integrity (CWI) sensors linking the different cellular compartments. LRR-eXtensins (LRXs) are cell wall-attached extracellular regulators of cell wall for...

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Autores principales: Herger, Aline, Gupta, Shibu, Kadler, Gabor, Franck, Christina Maria, Boisson-Dernier, Aurélien, Ringli, Christoph
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7357788/
https://www.ncbi.nlm.nih.gov/pubmed/32559234
http://dx.doi.org/10.1371/journal.pgen.1008847
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author Herger, Aline
Gupta, Shibu
Kadler, Gabor
Franck, Christina Maria
Boisson-Dernier, Aurélien
Ringli, Christoph
author_facet Herger, Aline
Gupta, Shibu
Kadler, Gabor
Franck, Christina Maria
Boisson-Dernier, Aurélien
Ringli, Christoph
author_sort Herger, Aline
collection PubMed
description Plant cell growth requires the coordinated expansion of the protoplast and the cell wall, which is controlled by an elaborate system of cell wall integrity (CWI) sensors linking the different cellular compartments. 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. LRXs function in CWI sensing and in the case of LRX4 of Arabidopsis thaliana, this activity was shown to involve interaction with the transmembrane Catharanthus roseus Receptor-Like Kinase1-Like (CrRLK1L) protein FERONIA (FER). Here, we demonstrate that binding of RALF1 and FER is common to most tested LRXs of vegetative tissue, including LRX1, the main LRX protein of root hairs. Consequently, an lrx1-lrx5 quintuple mutant line develops shoot and root phenotypes reminiscent of the fer-4 knock-out mutant. The previously observed membrane-association of LRXs, however, is FER-independent, suggesting that LRXs bind not only FER but also other membrane-localized proteins to establish a physical link between intra- and extracellular compartments. Despite evolutionary diversification of various LRX proteins, overexpression of several chimeric LRX constructs causes cross-complementation of lrx mutants, indicative of comparable functions among members of this protein family. Suppressors of the pollen-growth defects induced by mutations in the CrRLK1Ls ANXUR1/2 also alleviate lrx1 lrx2-induced mutant root hair phenotypes. This suggests functional similarity of LRX-CrRLK1L signaling processes in very different cell types and indicates that LRX proteins are components of conserved processes regulating cell growth.
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spelling pubmed-73577882020-07-22 Overlapping functions and protein-protein interactions of LRR-extensins in Arabidopsis Herger, Aline Gupta, Shibu Kadler, Gabor Franck, Christina Maria Boisson-Dernier, Aurélien Ringli, Christoph PLoS Genet Research Article Plant cell growth requires the coordinated expansion of the protoplast and the cell wall, which is controlled by an elaborate system of cell wall integrity (CWI) sensors linking the different cellular compartments. 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. LRXs function in CWI sensing and in the case of LRX4 of Arabidopsis thaliana, this activity was shown to involve interaction with the transmembrane Catharanthus roseus Receptor-Like Kinase1-Like (CrRLK1L) protein FERONIA (FER). Here, we demonstrate that binding of RALF1 and FER is common to most tested LRXs of vegetative tissue, including LRX1, the main LRX protein of root hairs. Consequently, an lrx1-lrx5 quintuple mutant line develops shoot and root phenotypes reminiscent of the fer-4 knock-out mutant. The previously observed membrane-association of LRXs, however, is FER-independent, suggesting that LRXs bind not only FER but also other membrane-localized proteins to establish a physical link between intra- and extracellular compartments. Despite evolutionary diversification of various LRX proteins, overexpression of several chimeric LRX constructs causes cross-complementation of lrx mutants, indicative of comparable functions among members of this protein family. Suppressors of the pollen-growth defects induced by mutations in the CrRLK1Ls ANXUR1/2 also alleviate lrx1 lrx2-induced mutant root hair phenotypes. This suggests functional similarity of LRX-CrRLK1L signaling processes in very different cell types and indicates that LRX proteins are components of conserved processes regulating cell growth. Public Library of Science 2020-06-19 /pmc/articles/PMC7357788/ /pubmed/32559234 http://dx.doi.org/10.1371/journal.pgen.1008847 Text en © 2020 Herger et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Herger, Aline
Gupta, Shibu
Kadler, Gabor
Franck, Christina Maria
Boisson-Dernier, Aurélien
Ringli, Christoph
Overlapping functions and protein-protein interactions of LRR-extensins in Arabidopsis
title Overlapping functions and protein-protein interactions of LRR-extensins in Arabidopsis
title_full Overlapping functions and protein-protein interactions of LRR-extensins in Arabidopsis
title_fullStr Overlapping functions and protein-protein interactions of LRR-extensins in Arabidopsis
title_full_unstemmed Overlapping functions and protein-protein interactions of LRR-extensins in Arabidopsis
title_short Overlapping functions and protein-protein interactions of LRR-extensins in Arabidopsis
title_sort overlapping functions and protein-protein interactions of lrr-extensins in arabidopsis
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7357788/
https://www.ncbi.nlm.nih.gov/pubmed/32559234
http://dx.doi.org/10.1371/journal.pgen.1008847
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