New roles for old friends: a microtubule-localized COP1-interacting protein promotes hypocotyl elongation in the dark

Autores
Arico, Denise Soledad; Wengier, Diego Leonardo; Castro, Luciana; Muschietti, Jorge Prometeo; Mazzella, Maria Agustina
Año de publicación
2019
Idioma
inglés
Tipo de recurso
documento de conferencia
Estado
versión publicada
Descripción
Plant irritability for light stimuli becomes crucial to cope with ambient fluctuations in order to keep up homeostasis and accomplish the life cyclesuccessfully. Light environment governs plant development. Perception of light is carried out by photoreceptors, such as phytochromes (phyA to phyE) that absorb primarily in red and far-red; and cryptochromes (cry1 to cry3) that are predominantly blue-light receptors. Once perceived, plants are able to integrate light signals into biochemical networks that conduce to proper response. Transducing these lightsignals involve changes in the phosphorylation state of proteins. In an early light-induced phosphoproteome study in Arabidopsis thaliana, we identified a protein that presents light-responsive dephosphorylation in the presence of photoactivated photoreceptors. This protein was particularly interesting because it was reported to interact with the key repressor of photomorphogenesis COP1 and thus, it is potentially involved in early photomorphogenesis events. In vivo assays with a transcriptional reporter revealed it is expressed in cotyledons and elongation zones of hypocotyl and root. Its expression is regulated negatively by light. CRISPR-CAS9 mutated lines exhibit shorter hypocotyls in darkness. Confocal microscopy assays with stably transgenic lines expressing translational reporters revealed localization to cortical microtubules. We are currently studying the biological implications of its microtubule association and its regulation by COP1 through changes in phosphorylation patterns. All these results suggest this protein promotes growth in darkness by affecting microtubules dynamics.
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: Castro, Luciana. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
Fil: Muschietti, Jorge Prometeo. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; 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
Joint LV Annual SAIB Meeting and XIV PABMB Congress
Salta
Argentina
Sociedad Argentina de Investigaciones en Bioquímica y Biología Molecular
Materia
PHOTOMORPHOGENESIS
PHOSPHORYLATION
MICROTUBULES
COP1-INTERACTING-PROTEIN
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/234316
Acceder
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repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling New roles for old friends: a microtubule-localized COP1-interacting protein promotes hypocotyl elongation in the darkArico, Denise SoledadWengier, Diego LeonardoCastro, LucianaMuschietti, Jorge PrometeoMazzella, Maria AgustinaPHOTOMORPHOGENESISPHOSPHORYLATIONMICROTUBULESCOP1-INTERACTING-PROTEINhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Plant irritability for light stimuli becomes crucial to cope with ambient fluctuations in order to keep up homeostasis and accomplish the life cyclesuccessfully. Light environment governs plant development. Perception of light is carried out by photoreceptors, such as phytochromes (phyA to phyE) that absorb primarily in red and far-red; and cryptochromes (cry1 to cry3) that are predominantly blue-light receptors. Once perceived, plants are able to integrate light signals into biochemical networks that conduce to proper response. Transducing these lightsignals involve changes in the phosphorylation state of proteins. In an early light-induced phosphoproteome study in Arabidopsis thaliana, we identified a protein that presents light-responsive dephosphorylation in the presence of photoactivated photoreceptors. This protein was particularly interesting because it was reported to interact with the key repressor of photomorphogenesis COP1 and thus, it is potentially involved in early photomorphogenesis events. In vivo assays with a transcriptional reporter revealed it is expressed in cotyledons and elongation zones of hypocotyl and root. Its expression is regulated negatively by light. CRISPR-CAS9 mutated lines exhibit shorter hypocotyls in darkness. Confocal microscopy assays with stably transgenic lines expressing translational reporters revealed localization to cortical microtubules. We are currently studying the biological implications of its microtubule association and its regulation by COP1 through changes in phosphorylation patterns. All these results suggest this protein promotes growth in darkness by affecting microtubules dynamics.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: Castro, Luciana. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; ArgentinaFil: Muschietti, Jorge Prometeo. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Mazzella, Maria Agustina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; ArgentinaJoint LV Annual SAIB Meeting and XIV PABMB CongressSaltaArgentinaSociedad Argentina de Investigaciones en Bioquímica y Biología MolecularTech Science Press2019info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectReuniónJournalhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/234316New roles for old friends: a microtubule-localized COP1-interacting protein promotes hypocotyl elongation in the dark; Joint LV Annual SAIB Meeting and XIV PABMB Congress; Salta; Argentina; 2019; 55-561667-5746CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.saib.org.ar/sites/default/files/BIOCELL-SAIB-2019-version-final.pdfInternacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:32:50Zoai:ri.conicet.gov.ar:11336/234316instacron: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:34982025-09-29 09:32:50.568CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv New roles for old friends: a microtubule-localized COP1-interacting protein promotes hypocotyl elongation in the dark
title New roles for old friends: a microtubule-localized COP1-interacting protein promotes hypocotyl elongation in the dark
spellingShingle New roles for old friends: a microtubule-localized COP1-interacting protein promotes hypocotyl elongation in the dark
Arico, Denise Soledad
PHOTOMORPHOGENESIS
PHOSPHORYLATION
MICROTUBULES
COP1-INTERACTING-PROTEIN
title_short New roles for old friends: a microtubule-localized COP1-interacting protein promotes hypocotyl elongation in the dark
title_full New roles for old friends: a microtubule-localized COP1-interacting protein promotes hypocotyl elongation in the dark
title_fullStr New roles for old friends: a microtubule-localized COP1-interacting protein promotes hypocotyl elongation in the dark
title_full_unstemmed New roles for old friends: a microtubule-localized COP1-interacting protein promotes hypocotyl elongation in the dark
title_sort New roles for old friends: a microtubule-localized COP1-interacting protein promotes hypocotyl elongation in the dark
dc.creator.none.fl_str_mv Arico, Denise Soledad
Wengier, Diego Leonardo
Castro, Luciana
Muschietti, Jorge Prometeo
Mazzella, Maria Agustina
author Arico, Denise Soledad
author_facet Arico, Denise Soledad
Wengier, Diego Leonardo
Castro, Luciana
Muschietti, Jorge Prometeo
Mazzella, Maria Agustina
author_role author
author2 Wengier, Diego Leonardo
Castro, Luciana
Muschietti, Jorge Prometeo
Mazzella, Maria Agustina
author2_role author
author
author
author
dc.subject.none.fl_str_mv PHOTOMORPHOGENESIS
PHOSPHORYLATION
MICROTUBULES
COP1-INTERACTING-PROTEIN
topic PHOTOMORPHOGENESIS
PHOSPHORYLATION
MICROTUBULES
COP1-INTERACTING-PROTEIN
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Plant irritability for light stimuli becomes crucial to cope with ambient fluctuations in order to keep up homeostasis and accomplish the life cyclesuccessfully. Light environment governs plant development. Perception of light is carried out by photoreceptors, such as phytochromes (phyA to phyE) that absorb primarily in red and far-red; and cryptochromes (cry1 to cry3) that are predominantly blue-light receptors. Once perceived, plants are able to integrate light signals into biochemical networks that conduce to proper response. Transducing these lightsignals involve changes in the phosphorylation state of proteins. In an early light-induced phosphoproteome study in Arabidopsis thaliana, we identified a protein that presents light-responsive dephosphorylation in the presence of photoactivated photoreceptors. This protein was particularly interesting because it was reported to interact with the key repressor of photomorphogenesis COP1 and thus, it is potentially involved in early photomorphogenesis events. In vivo assays with a transcriptional reporter revealed it is expressed in cotyledons and elongation zones of hypocotyl and root. Its expression is regulated negatively by light. CRISPR-CAS9 mutated lines exhibit shorter hypocotyls in darkness. Confocal microscopy assays with stably transgenic lines expressing translational reporters revealed localization to cortical microtubules. We are currently studying the biological implications of its microtubule association and its regulation by COP1 through changes in phosphorylation patterns. All these results suggest this protein promotes growth in darkness by affecting microtubules dynamics.
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: Castro, Luciana. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
Fil: Muschietti, Jorge Prometeo. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; 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
Joint LV Annual SAIB Meeting and XIV PABMB Congress
Salta
Argentina
Sociedad Argentina de Investigaciones en Bioquímica y Biología Molecular
description Plant irritability for light stimuli becomes crucial to cope with ambient fluctuations in order to keep up homeostasis and accomplish the life cyclesuccessfully. Light environment governs plant development. Perception of light is carried out by photoreceptors, such as phytochromes (phyA to phyE) that absorb primarily in red and far-red; and cryptochromes (cry1 to cry3) that are predominantly blue-light receptors. Once perceived, plants are able to integrate light signals into biochemical networks that conduce to proper response. Transducing these lightsignals involve changes in the phosphorylation state of proteins. In an early light-induced phosphoproteome study in Arabidopsis thaliana, we identified a protein that presents light-responsive dephosphorylation in the presence of photoactivated photoreceptors. This protein was particularly interesting because it was reported to interact with the key repressor of photomorphogenesis COP1 and thus, it is potentially involved in early photomorphogenesis events. In vivo assays with a transcriptional reporter revealed it is expressed in cotyledons and elongation zones of hypocotyl and root. Its expression is regulated negatively by light. CRISPR-CAS9 mutated lines exhibit shorter hypocotyls in darkness. Confocal microscopy assays with stably transgenic lines expressing translational reporters revealed localization to cortical microtubules. We are currently studying the biological implications of its microtubule association and its regulation by COP1 through changes in phosphorylation patterns. All these results suggest this protein promotes growth in darkness by affecting microtubules dynamics.
publishDate 2019
dc.date.none.fl_str_mv 2019
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/conferenceObject
Reunión
Journal
http://purl.org/coar/resource_type/c_5794
info:ar-repo/semantics/documentoDeConferencia
status_str publishedVersion
format conferenceObject
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/234316
New roles for old friends: a microtubule-localized COP1-interacting protein promotes hypocotyl elongation in the dark; Joint LV Annual SAIB Meeting and XIV PABMB Congress; Salta; Argentina; 2019; 55-56
1667-5746
CONICET Digital
CONICET
url http://hdl.handle.net/11336/234316
identifier_str_mv New roles for old friends: a microtubule-localized COP1-interacting protein promotes hypocotyl elongation in the dark; Joint LV Annual SAIB Meeting and XIV PABMB Congress; Salta; Argentina; 2019; 55-56
1667-5746
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.saib.org.ar/sites/default/files/BIOCELL-SAIB-2019-version-final.pdf
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.coverage.none.fl_str_mv Internacional
dc.publisher.none.fl_str_mv Tech Science Press
publisher.none.fl_str_mv Tech Science Press
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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