ABLs and TMKs are co-receptors for extracellular auxin
SUMMARY Extracellular perception of auxin, an essential phytohormone in plants, has been debated for decades. Auxin binding protein 1 (ABP1) physically interacts with quintessential transmembrane kinases (TMKs) and was proposed to act as an extracellular auxin receptor, but its role was disputed becauseabp1knockout mutants lack obvious morphological phenotypes. Here we identified two new auxin-binding proteins, ABL1 and ABL2, that are localized to the apoplast and directly interact with the extracellular domain of TMKs in an auxin-dependent manner. Furthermore, functionally redundant ABL1 and ABL2 genetically interact with TMKs and exhibit functions that are overlapping with those of ABP1 as well as independent of ABP1. Importantly, the extracellular domain of TMK1 itself binds auxin and synergizes with either ABP1 or ABL1 in auxin binding. Thus, our findings discovered new auxin receptors ABL1 and ABL2 having functions overlapping with but distinct from ABP1 and acting together with TMKs as co-receptors for extracellular auxin..
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Preprint| Erscheinungsjahr: |
2024 |
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| Erschienen: |
2024 |
| Enthalten in: |
bioRxiv.org - (2024) vom: 23. Apr. Zur Gesamtaufnahme - year:2024 |
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| Sprache: |
Englisch |
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| Beteiligte Personen: |
Yu, Yongqiang [VerfasserIn] |
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| doi: |
10.1101/2022.11.28.518138 |
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| PPN (Katalog-ID): |
XBI038011964 |
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| 245 | 1 | 0 | |a ABLs and TMKs are co-receptors for extracellular auxin |
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| 520 | |a SUMMARY Extracellular perception of auxin, an essential phytohormone in plants, has been debated for decades. Auxin binding protein 1 (ABP1) physically interacts with quintessential transmembrane kinases (TMKs) and was proposed to act as an extracellular auxin receptor, but its role was disputed becauseabp1knockout mutants lack obvious morphological phenotypes. Here we identified two new auxin-binding proteins, ABL1 and ABL2, that are localized to the apoplast and directly interact with the extracellular domain of TMKs in an auxin-dependent manner. Furthermore, functionally redundant ABL1 and ABL2 genetically interact with TMKs and exhibit functions that are overlapping with those of ABP1 as well as independent of ABP1. Importantly, the extracellular domain of TMK1 itself binds auxin and synergizes with either ABP1 or ABL1 in auxin binding. Thus, our findings discovered new auxin receptors ABL1 and ABL2 having functions overlapping with but distinct from ABP1 and acting together with TMKs as co-receptors for extracellular auxin. | ||
| 650 | 4 | |a Biology |7 (dpeaa)DE-84 | |
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| 700 | 1 | |a Tang, Wenxin |e verfasserin |4 aut | |
| 700 | 1 | |a Lin, Wenwei |e verfasserin |0 (orcid)0000-0003-0098-6386 |4 aut | |
| 700 | 1 | |a Li, Wei |e verfasserin |0 (orcid)0000-0001-9704-2044 |4 aut | |
| 700 | 1 | |a Zhou, Xiang |e verfasserin |4 aut | |
| 700 | 1 | |a Li, Ying |e verfasserin |4 aut | |
| 700 | 1 | |a Chen, Rong |e verfasserin |4 aut | |
| 700 | 1 | |a Zheng, Rui |e verfasserin |4 aut | |
| 700 | 1 | |a Qin, Guochen |e verfasserin |4 aut | |
| 700 | 1 | |a Cao, Wenhan |e verfasserin |4 aut | |
| 700 | 1 | |a Perez, Patricio |e verfasserin |4 aut | |
| 700 | 1 | |a Huang, Rongfeng |e verfasserin |4 aut | |
| 700 | 1 | |a Ma, Jun |e verfasserin |4 aut | |
| 700 | 1 | |a Lin, Juncheng |e verfasserin |4 aut | |
| 700 | 1 | |a Jiang, Liwen |e verfasserin |4 aut | |
| 700 | 1 | |a Xu, Tongda |e verfasserin |0 (orcid)0000-0003-3398-9217 |4 aut | |
| 700 | 1 | |a Yang, Zhenbiao |e verfasserin |0 (orcid)0000-0001-7482-6540 |4 aut | |
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