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M

M. L. Irigoyen

Researcher at Spanish National Research Council

Publications -  19
Citations -  1754

M. L. Irigoyen is an academic researcher from Spanish National Research Council. The author has contributed to research in topics: Genome & Arabidopsis. The author has an hindex of 13, co-authored 17 publications receiving 1468 citations. Previous affiliations of M. L. Irigoyen include University of Alcalá & University of California, Riverside.

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SPX1 is a phosphate-dependent inhibitor of PHOSPHATE STARVATION RESPONSE 1 in Arabidopsis

TL;DR: DNA-binding and pull-down assays showed that SPX1 is a competitive inhibitor of PHR1 binding to its recognition sequence, and that its efficiency is highly dependent on the presence of Pi or phosphite, a nonmetabolizable Pi analog that can repress PSRs.
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COP1 and ELF3 Control Circadian Function and Photoperiodic Flowering by Regulating GI Stability

TL;DR: It is shown that COP1 acts with ELF3 to mediate day length signaling from CRY2 to GI within the photoperiod flowering pathway, enabling COP1 to modulate light input signal to the circadian clock through targeted destabilization of GI.
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Plant hormones and nutrient signaling.

TL;DR: This review summarizes evidences and analyzes possible transcriptional correlations between hormonal and nutritional responses, as a means to further characterize the role of hormones in the response of plants to limiting nutrients in soil.
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LZF1/SALT TOLERANCE HOMOLOG3, an Arabidopsis B-box protein involved in light-dependent development and gene expression, undergoes COP1-mediated ubiquitination

TL;DR: STH3 is identified as a positive regulator of photomorphogenesis acting in concert with STH2 and HY5, while also being a target of COP1-mediated ubiquitination.
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Targeted Degradation of Abscisic Acid Receptors Is Mediated by the Ubiquitin Ligase Substrate Adaptor DDA1 in Arabidopsis

TL;DR: Evidence is provided that Arabidopsis thaliana DET1-, DDB1-ASSOCIATED1 (DDA1), as part of the CDD complex, provides substrate specificity for CRL4 by interacting with ubiquitination targets, and it is shown that DDA1 binds to the abscisic acid (ABA) receptor PYL8, as well as PYL4 and PYL9, in vivo and facilitates its proteasomal degradation.