The receptor kinases LePRK1 and LePRK2 associate in pollen and when expressed in yeast, but dissociate in the presence of style extract
After pollen grains germinate on the stigma, pollen tubes traverse the extracellular matrix of the style on their way to the ovules. We previously characterized two pollen-specific, receptor-like kinases, LePRK1 and LePRK2, from tomato (Lycopersicon esculentum). Their structure and immunolocalizatio...
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2003
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00278424_v100_n11_p6860_Wengier http://hdl.handle.net/20.500.12110/paper_00278424_v100_n11_p6860_Wengier |
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paper:paper_00278424_v100_n11_p6860_Wengier2023-06-08T14:54:18Z The receptor kinases LePRK1 and LePRK2 associate in pollen and when expressed in yeast, but dissociate in the presence of style extract plant extract protein kinase protein LePRK1 protein LePRK2 unclassified drug article autophosphorylation dephosphorylation dissociation enzyme activity extracellular matrix fractionation germination immunoprecipitation molecular interaction nonhuman pistil style pollen pollen tube priority journal protein expression protein stability signal transduction thermostability tomato yeast Lycopersicon esculentum Pollen Protein Kinase C Recombinant Proteins Saccharomyces cerevisiae Fungi Lycopersicon Lycopersicon esculentum After pollen grains germinate on the stigma, pollen tubes traverse the extracellular matrix of the style on their way to the ovules. We previously characterized two pollen-specific, receptor-like kinases, LePRK1 and LePRK2, from tomato (Lycopersicon esculentum). Their structure and immunolocalization pattern and the specific dephosphorylation of LePRK2 suggested that these kinases might interact with signaling molecules in the style extracellular matrix. Here, we show that LePRK1 and LePRK2 can be coimmunoprecipitated from pollen or when expressed together in yeast. In yeast, their association requires LePRK2 kinase activity. In pollen, LePRK1 and LePRK2 are found in an ≈400-kDa protein complex that persists on pollen germination, but this complex is disrupted when pollen is germinated in vitro in the presence of style extract. In yeast, the addition of style extract also disrupts the interaction between LePRK1 and LePRK2. Fractionation of the style extract reveals that the disruption activity is enriched in the 3- to 10-kDa fraction. A component(s) in this fraction also is responsible for the specific dephosphorylation of LePRK2. The style component(s) that dephosphorylates LePRK2 is likely to be a heat-stable peptide that is present in exudate from the style. The generally accepted model of receptor kinase signaling involves binding of a ligand to extracellular domains of receptor kinases and subsequent activation of the signaling pathway by receptor autophosphorylation. In contrast to this typical scenario, we propose that a putative style ligand transduces the signal in pollen tubes by triggering the specific dephosphorylation of LePRK2, followed by dissociation of the LePRK complex. 2003 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00278424_v100_n11_p6860_Wengier http://hdl.handle.net/20.500.12110/paper_00278424_v100_n11_p6860_Wengier |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
plant extract protein kinase protein LePRK1 protein LePRK2 unclassified drug article autophosphorylation dephosphorylation dissociation enzyme activity extracellular matrix fractionation germination immunoprecipitation molecular interaction nonhuman pistil style pollen pollen tube priority journal protein expression protein stability signal transduction thermostability tomato yeast Lycopersicon esculentum Pollen Protein Kinase C Recombinant Proteins Saccharomyces cerevisiae Fungi Lycopersicon Lycopersicon esculentum |
| spellingShingle |
plant extract protein kinase protein LePRK1 protein LePRK2 unclassified drug article autophosphorylation dephosphorylation dissociation enzyme activity extracellular matrix fractionation germination immunoprecipitation molecular interaction nonhuman pistil style pollen pollen tube priority journal protein expression protein stability signal transduction thermostability tomato yeast Lycopersicon esculentum Pollen Protein Kinase C Recombinant Proteins Saccharomyces cerevisiae Fungi Lycopersicon Lycopersicon esculentum The receptor kinases LePRK1 and LePRK2 associate in pollen and when expressed in yeast, but dissociate in the presence of style extract |
| topic_facet |
plant extract protein kinase protein LePRK1 protein LePRK2 unclassified drug article autophosphorylation dephosphorylation dissociation enzyme activity extracellular matrix fractionation germination immunoprecipitation molecular interaction nonhuman pistil style pollen pollen tube priority journal protein expression protein stability signal transduction thermostability tomato yeast Lycopersicon esculentum Pollen Protein Kinase C Recombinant Proteins Saccharomyces cerevisiae Fungi Lycopersicon Lycopersicon esculentum |
| description |
After pollen grains germinate on the stigma, pollen tubes traverse the extracellular matrix of the style on their way to the ovules. We previously characterized two pollen-specific, receptor-like kinases, LePRK1 and LePRK2, from tomato (Lycopersicon esculentum). Their structure and immunolocalization pattern and the specific dephosphorylation of LePRK2 suggested that these kinases might interact with signaling molecules in the style extracellular matrix. Here, we show that LePRK1 and LePRK2 can be coimmunoprecipitated from pollen or when expressed together in yeast. In yeast, their association requires LePRK2 kinase activity. In pollen, LePRK1 and LePRK2 are found in an ≈400-kDa protein complex that persists on pollen germination, but this complex is disrupted when pollen is germinated in vitro in the presence of style extract. In yeast, the addition of style extract also disrupts the interaction between LePRK1 and LePRK2. Fractionation of the style extract reveals that the disruption activity is enriched in the 3- to 10-kDa fraction. A component(s) in this fraction also is responsible for the specific dephosphorylation of LePRK2. The style component(s) that dephosphorylates LePRK2 is likely to be a heat-stable peptide that is present in exudate from the style. The generally accepted model of receptor kinase signaling involves binding of a ligand to extracellular domains of receptor kinases and subsequent activation of the signaling pathway by receptor autophosphorylation. In contrast to this typical scenario, we propose that a putative style ligand transduces the signal in pollen tubes by triggering the specific dephosphorylation of LePRK2, followed by dissociation of the LePRK complex. |
| title |
The receptor kinases LePRK1 and LePRK2 associate in pollen and when expressed in yeast, but dissociate in the presence of style extract |
| title_short |
The receptor kinases LePRK1 and LePRK2 associate in pollen and when expressed in yeast, but dissociate in the presence of style extract |
| title_full |
The receptor kinases LePRK1 and LePRK2 associate in pollen and when expressed in yeast, but dissociate in the presence of style extract |
| title_fullStr |
The receptor kinases LePRK1 and LePRK2 associate in pollen and when expressed in yeast, but dissociate in the presence of style extract |
| title_full_unstemmed |
The receptor kinases LePRK1 and LePRK2 associate in pollen and when expressed in yeast, but dissociate in the presence of style extract |
| title_sort |
receptor kinases leprk1 and leprk2 associate in pollen and when expressed in yeast, but dissociate in the presence of style extract |
| publishDate |
2003 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00278424_v100_n11_p6860_Wengier http://hdl.handle.net/20.500.12110/paper_00278424_v100_n11_p6860_Wengier |
| _version_ |
1768542162855657472 |