Glycosylphosphatidylinositol-anchored proteins as chaperones and co-receptors for FERONIA receptor kinase signaling in Arabidopsis
The Arabidopsis receptor kinase FERONIA (FER) is a multifunctional regulator for plant growth and reproduction. Here we report that the female gametophyte-expressed glycosylphosphatidylinositol-anchored protein (GPI-AP) LORELEI and the seedling-expressed LRE-like GPI-AP1 (LLG1) bind to the extracell...
| Main Authors: | , , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2015-06-01
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| Series: | eLife |
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| Online Access: | https://elifesciences.org/articles/06587 |
| _version_ | 1811200112018325504 |
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| author | Chao Li Fang-Ling Yeh Alice Y Cheung Qiaohong Duan Daniel Kita Ming-Che Liu Jacob Maman Emily J Luu Brendan W Wu Laura Gates Methun Jalal Amy Kwong Hunter Carpenter Hen-Ming Wu |
| author_facet | Chao Li Fang-Ling Yeh Alice Y Cheung Qiaohong Duan Daniel Kita Ming-Che Liu Jacob Maman Emily J Luu Brendan W Wu Laura Gates Methun Jalal Amy Kwong Hunter Carpenter Hen-Ming Wu |
| author_sort | Chao Li |
| collection | DOAJ |
| description | The Arabidopsis receptor kinase FERONIA (FER) is a multifunctional regulator for plant growth and reproduction. Here we report that the female gametophyte-expressed glycosylphosphatidylinositol-anchored protein (GPI-AP) LORELEI and the seedling-expressed LRE-like GPI-AP1 (LLG1) bind to the extracellular juxtamembrane region of FER and show that this interaction is pivotal for FER function. LLG1 interacts with FER in the endoplasmic reticulum and on the cell surface, and loss of LLG1 function induces cytoplasmic retention of FER, consistent with transport of FER from the endoplasmic reticulum to the plasma membrane in a complex with LLG1. We further demonstrate that LLG1 is a component of the FER-regulated RHO GTPase signaling complex and that fer and llg1 mutants display indistinguishable growth, developmental and signaling phenotypes, analogous to how lre and fer share similar reproductive defects. Together our results support LLG1/LRE acting as a chaperone and co-receptor for FER and elucidate a mechanism by which GPI-APs enable the signaling capacity of a cell surface receptor. |
| first_indexed | 2024-04-12T01:59:18Z |
| format | Article |
| id | doaj.art-7c0af066ef0e4d6482463303e4e8a905 |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-12T01:59:18Z |
| publishDate | 2015-06-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-7c0af066ef0e4d6482463303e4e8a9052022-12-22T03:52:44ZengeLife Sciences Publications LtdeLife2050-084X2015-06-01410.7554/eLife.06587Glycosylphosphatidylinositol-anchored proteins as chaperones and co-receptors for FERONIA receptor kinase signaling in ArabidopsisChao Li0Fang-Ling Yeh1Alice Y Cheung2https://orcid.org/0000-0002-7973-022XQiaohong Duan3Daniel Kita4Ming-Che Liu5Jacob Maman6Emily J Luu7Brendan W Wu8Laura Gates9Methun Jalal10Amy Kwong11Hunter Carpenter12Hen-Ming Wu13Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, United StatesDepartment of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, United StatesDepartment of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, United States; Molecular and Cell Biology Program, University of Massachusetts, Amherst, United States; Plant Biology Graduate Program, University of Massachusetts, Amherst, United StatesDepartment of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, United StatesDepartment of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, United States; Molecular and Cell Biology Program, University of Massachusetts, Amherst, United StatesDepartment of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, United States; Graduate Institute of Biotechnology, National Chung Hsing University, Tai Chung, TaiwanDepartment of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, United StatesDepartment of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, United StatesDepartment of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, United StatesDepartment of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, United StatesDepartment of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, United StatesDepartment of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, United StatesDepartment of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, United StatesDepartment of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, United States; Molecular and Cell Biology Program, University of Massachusetts, Amherst, United StatesThe Arabidopsis receptor kinase FERONIA (FER) is a multifunctional regulator for plant growth and reproduction. Here we report that the female gametophyte-expressed glycosylphosphatidylinositol-anchored protein (GPI-AP) LORELEI and the seedling-expressed LRE-like GPI-AP1 (LLG1) bind to the extracellular juxtamembrane region of FER and show that this interaction is pivotal for FER function. LLG1 interacts with FER in the endoplasmic reticulum and on the cell surface, and loss of LLG1 function induces cytoplasmic retention of FER, consistent with transport of FER from the endoplasmic reticulum to the plasma membrane in a complex with LLG1. We further demonstrate that LLG1 is a component of the FER-regulated RHO GTPase signaling complex and that fer and llg1 mutants display indistinguishable growth, developmental and signaling phenotypes, analogous to how lre and fer share similar reproductive defects. Together our results support LLG1/LRE acting as a chaperone and co-receptor for FER and elucidate a mechanism by which GPI-APs enable the signaling capacity of a cell surface receptor.https://elifesciences.org/articles/06587malectin domain-containing receptor kinaseFERONIA as coreceptorreceptor kinase and GPI-AP as functional partnerplant Rho GTPase signalingRALFLORELEI/LLG1 as coreceptor |
| spellingShingle | Chao Li Fang-Ling Yeh Alice Y Cheung Qiaohong Duan Daniel Kita Ming-Che Liu Jacob Maman Emily J Luu Brendan W Wu Laura Gates Methun Jalal Amy Kwong Hunter Carpenter Hen-Ming Wu Glycosylphosphatidylinositol-anchored proteins as chaperones and co-receptors for FERONIA receptor kinase signaling in Arabidopsis eLife malectin domain-containing receptor kinase FERONIA as coreceptor receptor kinase and GPI-AP as functional partner plant Rho GTPase signaling RALF LORELEI/LLG1 as coreceptor |
| title | Glycosylphosphatidylinositol-anchored proteins as chaperones and co-receptors for FERONIA receptor kinase signaling in Arabidopsis |
| title_full | Glycosylphosphatidylinositol-anchored proteins as chaperones and co-receptors for FERONIA receptor kinase signaling in Arabidopsis |
| title_fullStr | Glycosylphosphatidylinositol-anchored proteins as chaperones and co-receptors for FERONIA receptor kinase signaling in Arabidopsis |
| title_full_unstemmed | Glycosylphosphatidylinositol-anchored proteins as chaperones and co-receptors for FERONIA receptor kinase signaling in Arabidopsis |
| title_short | Glycosylphosphatidylinositol-anchored proteins as chaperones and co-receptors for FERONIA receptor kinase signaling in Arabidopsis |
| title_sort | glycosylphosphatidylinositol anchored proteins as chaperones and co receptors for feronia receptor kinase signaling in arabidopsis |
| topic | malectin domain-containing receptor kinase FERONIA as coreceptor receptor kinase and GPI-AP as functional partner plant Rho GTPase signaling RALF LORELEI/LLG1 as coreceptor |
| url | https://elifesciences.org/articles/06587 |
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