Radip light-induced phosphorylation changes in microtubule related proteins in arabidopsis
- Autores
- Arico, Denise Soledad; Wengier, Diego Leonardo; Burachik, Natalia Belén; Mazzella, Maria Agustina
- Año de publicación
- 2023
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Rapid hypocotyl elongation allows buried seedlings to reach the surface, where light triggers de-etiolation and inhibits hypocotyl growth mainly by phytochromes A, B and cryptochromes 1, 2. Dynamic phosphorylation/dephosphorylation events provide a mechanism to rapidly transduce light signals. Only recently we have begun to uncover the earliest phospho-signaling responders to light.Here, we report a large-scale phosphoproteomic analysis and identify 20 proteins that change their phosphorylation pattern after 20 min of white light pulse compared to darkness. Microtubule-associated proteins (MAPs) were highly overrepresented in this group. Among them, we studied CIP7 (COP1-INTERACTING-PROTEIN-7), which presented microtubule (MT) localization, in contrast to what was previously described. Phosphorylated isoform in Serine 915 (Sp915) of CIP7 was detected in etiolated seedlings but undetectable after a light pulse in the presence of photoreceptors, while its expression decays with long light exposure.
Fil: Arico, Denise Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
Fil: Wengier, Diego Leonardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
Fil: Burachik, Natalia Belén. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
Fil: Mazzella, Maria Agustina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina - Materia
-
ARABIDOPSIS
LIGHT
MICROTUBULE
PHOSPHORYLATION - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
.jpg)
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/242593
Ver los metadatos del registro completo
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Radip light-induced phosphorylation changes in microtubule related proteins in arabidopsisArico, Denise SoledadWengier, Diego LeonardoBurachik, Natalia BelénMazzella, Maria AgustinaARABIDOPSISLIGHTMICROTUBULEPHOSPHORYLATIONhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Rapid hypocotyl elongation allows buried seedlings to reach the surface, where light triggers de-etiolation and inhibits hypocotyl growth mainly by phytochromes A, B and cryptochromes 1, 2. Dynamic phosphorylation/dephosphorylation events provide a mechanism to rapidly transduce light signals. Only recently we have begun to uncover the earliest phospho-signaling responders to light.Here, we report a large-scale phosphoproteomic analysis and identify 20 proteins that change their phosphorylation pattern after 20 min of white light pulse compared to darkness. Microtubule-associated proteins (MAPs) were highly overrepresented in this group. Among them, we studied CIP7 (COP1-INTERACTING-PROTEIN-7), which presented microtubule (MT) localization, in contrast to what was previously described. Phosphorylated isoform in Serine 915 (Sp915) of CIP7 was detected in etiolated seedlings but undetectable after a light pulse in the presence of photoreceptors, while its expression decays with long light exposure.Fil: Arico, Denise Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; ArgentinaFil: Wengier, Diego Leonardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; ArgentinaFil: Burachik, Natalia Belén. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; ArgentinaFil: Mazzella, Maria Agustina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; ArgentinaCold Spring Harbor Laboratory2023-05-31info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/242593Arico, Denise Soledad; Wengier, Diego Leonardo; Burachik, Natalia Belén; Mazzella, Maria Agustina; Radip light-induced phosphorylation changes in microtubule related proteins in arabidopsis; Cold Spring Harbor Laboratory; BioRxiv; 31-5-2023; 1-342692-82052692-8205CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.biorxiv.org/content/10.1101/2023.05.30.542878v1info:eu-repo/semantics/altIdentifier/doi/10.1101/2023.05.30.542878info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-11-12T09:55:55Zoai:ri.conicet.gov.ar:11336/242593instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-11-12 09:55:55.835CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
| dc.title.none.fl_str_mv |
Radip light-induced phosphorylation changes in microtubule related proteins in arabidopsis |
| title |
Radip light-induced phosphorylation changes in microtubule related proteins in arabidopsis |
| spellingShingle |
Radip light-induced phosphorylation changes in microtubule related proteins in arabidopsis Arico, Denise Soledad ARABIDOPSIS LIGHT MICROTUBULE PHOSPHORYLATION |
| title_short |
Radip light-induced phosphorylation changes in microtubule related proteins in arabidopsis |
| title_full |
Radip light-induced phosphorylation changes in microtubule related proteins in arabidopsis |
| title_fullStr |
Radip light-induced phosphorylation changes in microtubule related proteins in arabidopsis |
| title_full_unstemmed |
Radip light-induced phosphorylation changes in microtubule related proteins in arabidopsis |
| title_sort |
Radip light-induced phosphorylation changes in microtubule related proteins in arabidopsis |
| dc.creator.none.fl_str_mv |
Arico, Denise Soledad Wengier, Diego Leonardo Burachik, Natalia Belén Mazzella, Maria Agustina |
| author |
Arico, Denise Soledad |
| author_facet |
Arico, Denise Soledad Wengier, Diego Leonardo Burachik, Natalia Belén Mazzella, Maria Agustina |
| author_role |
author |
| author2 |
Wengier, Diego Leonardo Burachik, Natalia Belén Mazzella, Maria Agustina |
| author2_role |
author author author |
| dc.subject.none.fl_str_mv |
ARABIDOPSIS LIGHT MICROTUBULE PHOSPHORYLATION |
| topic |
ARABIDOPSIS LIGHT MICROTUBULE PHOSPHORYLATION |
| purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
| dc.description.none.fl_txt_mv |
Rapid hypocotyl elongation allows buried seedlings to reach the surface, where light triggers de-etiolation and inhibits hypocotyl growth mainly by phytochromes A, B and cryptochromes 1, 2. Dynamic phosphorylation/dephosphorylation events provide a mechanism to rapidly transduce light signals. Only recently we have begun to uncover the earliest phospho-signaling responders to light.Here, we report a large-scale phosphoproteomic analysis and identify 20 proteins that change their phosphorylation pattern after 20 min of white light pulse compared to darkness. Microtubule-associated proteins (MAPs) were highly overrepresented in this group. Among them, we studied CIP7 (COP1-INTERACTING-PROTEIN-7), which presented microtubule (MT) localization, in contrast to what was previously described. Phosphorylated isoform in Serine 915 (Sp915) of CIP7 was detected in etiolated seedlings but undetectable after a light pulse in the presence of photoreceptors, while its expression decays with long light exposure. Fil: Arico, Denise Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina Fil: Wengier, Diego Leonardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina Fil: Burachik, Natalia Belén. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina Fil: Mazzella, Maria Agustina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina |
| description |
Rapid hypocotyl elongation allows buried seedlings to reach the surface, where light triggers de-etiolation and inhibits hypocotyl growth mainly by phytochromes A, B and cryptochromes 1, 2. Dynamic phosphorylation/dephosphorylation events provide a mechanism to rapidly transduce light signals. Only recently we have begun to uncover the earliest phospho-signaling responders to light.Here, we report a large-scale phosphoproteomic analysis and identify 20 proteins that change their phosphorylation pattern after 20 min of white light pulse compared to darkness. Microtubule-associated proteins (MAPs) were highly overrepresented in this group. Among them, we studied CIP7 (COP1-INTERACTING-PROTEIN-7), which presented microtubule (MT) localization, in contrast to what was previously described. Phosphorylated isoform in Serine 915 (Sp915) of CIP7 was detected in etiolated seedlings but undetectable after a light pulse in the presence of photoreceptors, while its expression decays with long light exposure. |
| publishDate |
2023 |
| dc.date.none.fl_str_mv |
2023-05-31 |
| dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
| format |
article |
| status_str |
publishedVersion |
| dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/242593 Arico, Denise Soledad; Wengier, Diego Leonardo; Burachik, Natalia Belén; Mazzella, Maria Agustina; Radip light-induced phosphorylation changes in microtubule related proteins in arabidopsis; Cold Spring Harbor Laboratory; BioRxiv; 31-5-2023; 1-34 2692-8205 2692-8205 CONICET Digital CONICET |
| url |
http://hdl.handle.net/11336/242593 |
| identifier_str_mv |
Arico, Denise Soledad; Wengier, Diego Leonardo; Burachik, Natalia Belén; Mazzella, Maria Agustina; Radip light-induced phosphorylation changes in microtubule related proteins in arabidopsis; Cold Spring Harbor Laboratory; BioRxiv; 31-5-2023; 1-34 2692-8205 CONICET Digital CONICET |
| dc.language.none.fl_str_mv |
eng |
| language |
eng |
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info:eu-repo/semantics/altIdentifier/url/https://www.biorxiv.org/content/10.1101/2023.05.30.542878v1 info:eu-repo/semantics/altIdentifier/doi/10.1101/2023.05.30.542878 |
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openAccess |
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application/pdf application/pdf |
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Cold Spring Harbor Laboratory |
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Cold Spring Harbor Laboratory |
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CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
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dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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