The Evolutionarily Conserved Serine Residues in BRI1 LRR Motifs Are Critical for Protein Secretion
As a well-studied leucine-rich-repeat receptor-like kinases (LRR-RLKs) in Arabidopsis (Arabidopsis thaliana), BRI1 functions as a cell surface receptor for sensing the smallest ligand molecule identified thus far. The weak allele bri1-9 (S662F) harbors a mutation at the conserved serine (Ser*) resid...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2020-02-01
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| Series: | Frontiers in Plant Science |
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| Online Access: | https://www.frontiersin.org/article/10.3389/fpls.2020.00032/full |
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| author | Tianshu Chen Bin Wang Fangfang Wang Guanting Niu Shuo Zhang Jianming Li Jianming Li Zhi Hong |
| author_facet | Tianshu Chen Bin Wang Fangfang Wang Guanting Niu Shuo Zhang Jianming Li Jianming Li Zhi Hong |
| author_sort | Tianshu Chen |
| collection | DOAJ |
| description | As a well-studied leucine-rich-repeat receptor-like kinases (LRR-RLKs) in Arabidopsis (Arabidopsis thaliana), BRI1 functions as a cell surface receptor for sensing the smallest ligand molecule identified thus far. The weak allele bri1-9 (S662F) harbors a mutation at the conserved serine (Ser*) residue among 25 LRRs, which leads to the protein retention in the ER. However, very little is known about the importance of these residues. Through site-directed mutagenesis and a phenotypic complementation test, we examined the effects of these conserved serine residues (S*-chain) on protein secretion and functions. The results showed that the replacements of these serine residues significantly changed the sub-localization of BRI1-GFPs to the ER and that rigid space constraints, as well as the requirement of successive inner polar contacts, affect these sites. In addition, the continuous presence of Ser* is mainly disrupted at the LRR-island domain interface, and the changes of these four nonserine residues to serine greatly decreased the protein ability to complement bri1-301 compact phenotype and the BR signaling activation. The sequence alignment revealed that other known LRR-RLK also harbors the S*-chain and the non-Ser* residues at the ligand-binding region along the S*-chain, which confirms the evolutionary significance of residues at these sites in plant LRR-RLKs. |
| first_indexed | 2024-12-11T07:33:19Z |
| format | Article |
| id | doaj.art-78b1118a005949198ad00902d4c835f4 |
| institution | Directory Open Access Journal |
| issn | 1664-462X |
| language | English |
| last_indexed | 2024-12-11T07:33:19Z |
| publishDate | 2020-02-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Plant Science |
| spelling | doaj.art-78b1118a005949198ad00902d4c835f42022-12-22T01:15:45ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2020-02-011110.3389/fpls.2020.00032495498The Evolutionarily Conserved Serine Residues in BRI1 LRR Motifs Are Critical for Protein SecretionTianshu Chen0Bin Wang1Fangfang Wang2Guanting Niu3Shuo Zhang4Jianming Li5Jianming Li6Zhi Hong7State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing University, Nanjing, ChinaState Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing University, Nanjing, ChinaState Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing University, Nanjing, ChinaState Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing University, Nanjing, ChinaState Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing University, Nanjing, ChinaDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI, United StatesCollege of Forestry and Landscape Architecture, South China Agricultural University, Guangzhou, ChinaState Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing University, Nanjing, ChinaAs a well-studied leucine-rich-repeat receptor-like kinases (LRR-RLKs) in Arabidopsis (Arabidopsis thaliana), BRI1 functions as a cell surface receptor for sensing the smallest ligand molecule identified thus far. The weak allele bri1-9 (S662F) harbors a mutation at the conserved serine (Ser*) residue among 25 LRRs, which leads to the protein retention in the ER. However, very little is known about the importance of these residues. Through site-directed mutagenesis and a phenotypic complementation test, we examined the effects of these conserved serine residues (S*-chain) on protein secretion and functions. The results showed that the replacements of these serine residues significantly changed the sub-localization of BRI1-GFPs to the ER and that rigid space constraints, as well as the requirement of successive inner polar contacts, affect these sites. In addition, the continuous presence of Ser* is mainly disrupted at the LRR-island domain interface, and the changes of these four nonserine residues to serine greatly decreased the protein ability to complement bri1-301 compact phenotype and the BR signaling activation. The sequence alignment revealed that other known LRR-RLK also harbors the S*-chain and the non-Ser* residues at the ligand-binding region along the S*-chain, which confirms the evolutionary significance of residues at these sites in plant LRR-RLKs.https://www.frontiersin.org/article/10.3389/fpls.2020.00032/fullleucine-rich-repeat receptor-like kinasesBRI1evolutionArabidopsis thalianaprotein secretionBR signaling |
| spellingShingle | Tianshu Chen Bin Wang Fangfang Wang Guanting Niu Shuo Zhang Jianming Li Jianming Li Zhi Hong The Evolutionarily Conserved Serine Residues in BRI1 LRR Motifs Are Critical for Protein Secretion Frontiers in Plant Science leucine-rich-repeat receptor-like kinases BRI1 evolution Arabidopsis thaliana protein secretion BR signaling |
| title | The Evolutionarily Conserved Serine Residues in BRI1 LRR Motifs Are Critical for Protein Secretion |
| title_full | The Evolutionarily Conserved Serine Residues in BRI1 LRR Motifs Are Critical for Protein Secretion |
| title_fullStr | The Evolutionarily Conserved Serine Residues in BRI1 LRR Motifs Are Critical for Protein Secretion |
| title_full_unstemmed | The Evolutionarily Conserved Serine Residues in BRI1 LRR Motifs Are Critical for Protein Secretion |
| title_short | The Evolutionarily Conserved Serine Residues in BRI1 LRR Motifs Are Critical for Protein Secretion |
| title_sort | evolutionarily conserved serine residues in bri1 lrr motifs are critical for protein secretion |
| topic | leucine-rich-repeat receptor-like kinases BRI1 evolution Arabidopsis thaliana protein secretion BR signaling |
| url | https://www.frontiersin.org/article/10.3389/fpls.2020.00032/full |
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