Artículo
Radip light-induced phosphorylation changes in microtubule related proteins in arabidopsis
Fecha de publicación:
31/05/2023
Editorial:
Cold Spring Harbor Laboratory
Revista:
BioRxiv
ISSN:
2692-8205
e-ISSN:
2692-8205
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
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.
Palabras clave:
ARABIDOPSIS
,
LIGHT
,
MICROTUBULE
,
PHOSPHORYLATION
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Articulos(INGEBI)
Articulos de INST.DE INVEST.EN ING.GENETICA Y BIOL.MOLECULAR "DR. HECTOR N TORRES"
Articulos de INST.DE INVEST.EN ING.GENETICA Y BIOL.MOLECULAR "DR. HECTOR N TORRES"
Citación
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
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