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Malectin/Malectin-like domain-containing proteins: A repertoire of cell surface molecules with broad functional potential
Cell walls are at the front line of interactions between walled-organisms and their environment. They support cell expansion, ensure cell integrity and, for multicellular organisms such as plants, they provide cell adherence, support cell shape morphogenesis and mediate cell–cell communication. Wall...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8287233/ https://www.ncbi.nlm.nih.gov/pubmed/34308005 http://dx.doi.org/10.1016/j.tcsw.2021.100056 |
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author | Yang, He Wang, Dong Guo, Li Pan, Huairong Yvon, Robert Garman, Scott Wu, Hen-Ming Cheung, Alice Y. |
author_facet | Yang, He Wang, Dong Guo, Li Pan, Huairong Yvon, Robert Garman, Scott Wu, Hen-Ming Cheung, Alice Y. |
author_sort | Yang, He |
collection | PubMed |
description | Cell walls are at the front line of interactions between walled-organisms and their environment. They support cell expansion, ensure cell integrity and, for multicellular organisms such as plants, they provide cell adherence, support cell shape morphogenesis and mediate cell–cell communication. Wall-sensing, detecting perturbations in the wall and signaling the cell to respond accordingly, is crucial for growth and survival. In recent years, plant signaling research has suggested that a large family of receptor-like kinases (RLKs) could function as wall sensors partly because their extracellular domains show homology with malectin, a diglucose binding protein from the endoplasmic reticulum of animal cells. Studies of several malectin/malectin-like (M/ML) domain-containing RLKs (M/MLD-RLKs) from the model plant Arabidopsis thaliana have revealed an impressive array of biological roles, controlling growth, reproduction and stress responses, processes that in various ways rely on or affect the cell wall. Malectin homologous sequences are widespread across biological kingdoms, but plants have uniquely evolved a highly expanded family of proteins with ML domains embedded within various protein contexts. Here, we present an overview on proteins with malectin homologous sequences in different kingdoms, discuss the chromosomal organization of Arabidopsis M/MLD-RLKs and the phylogenetic relationship between these proteins from several model and crop species. We also discuss briefly the molecular networks that enable the diverse biological roles served by M/MLD-RLKs studied thus far. |
format | Online Article Text |
id | pubmed-8287233 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-82872332021-07-22 Malectin/Malectin-like domain-containing proteins: A repertoire of cell surface molecules with broad functional potential Yang, He Wang, Dong Guo, Li Pan, Huairong Yvon, Robert Garman, Scott Wu, Hen-Ming Cheung, Alice Y. Cell Surf Article Cell walls are at the front line of interactions between walled-organisms and their environment. They support cell expansion, ensure cell integrity and, for multicellular organisms such as plants, they provide cell adherence, support cell shape morphogenesis and mediate cell–cell communication. Wall-sensing, detecting perturbations in the wall and signaling the cell to respond accordingly, is crucial for growth and survival. In recent years, plant signaling research has suggested that a large family of receptor-like kinases (RLKs) could function as wall sensors partly because their extracellular domains show homology with malectin, a diglucose binding protein from the endoplasmic reticulum of animal cells. Studies of several malectin/malectin-like (M/ML) domain-containing RLKs (M/MLD-RLKs) from the model plant Arabidopsis thaliana have revealed an impressive array of biological roles, controlling growth, reproduction and stress responses, processes that in various ways rely on or affect the cell wall. Malectin homologous sequences are widespread across biological kingdoms, but plants have uniquely evolved a highly expanded family of proteins with ML domains embedded within various protein contexts. Here, we present an overview on proteins with malectin homologous sequences in different kingdoms, discuss the chromosomal organization of Arabidopsis M/MLD-RLKs and the phylogenetic relationship between these proteins from several model and crop species. We also discuss briefly the molecular networks that enable the diverse biological roles served by M/MLD-RLKs studied thus far. Elsevier 2021-06-24 /pmc/articles/PMC8287233/ /pubmed/34308005 http://dx.doi.org/10.1016/j.tcsw.2021.100056 Text en © 2021 The Authors https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Article Yang, He Wang, Dong Guo, Li Pan, Huairong Yvon, Robert Garman, Scott Wu, Hen-Ming Cheung, Alice Y. Malectin/Malectin-like domain-containing proteins: A repertoire of cell surface molecules with broad functional potential |
title | Malectin/Malectin-like domain-containing proteins: A repertoire of cell surface molecules with broad functional potential |
title_full | Malectin/Malectin-like domain-containing proteins: A repertoire of cell surface molecules with broad functional potential |
title_fullStr | Malectin/Malectin-like domain-containing proteins: A repertoire of cell surface molecules with broad functional potential |
title_full_unstemmed | Malectin/Malectin-like domain-containing proteins: A repertoire of cell surface molecules with broad functional potential |
title_short | Malectin/Malectin-like domain-containing proteins: A repertoire of cell surface molecules with broad functional potential |
title_sort | malectin/malectin-like domain-containing proteins: a repertoire of cell surface molecules with broad functional potential |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8287233/ https://www.ncbi.nlm.nih.gov/pubmed/34308005 http://dx.doi.org/10.1016/j.tcsw.2021.100056 |
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