- Plant Reproductive Biology
- Photosynthetic Processes and Mechanisms
- Cellular transport and secretion
- Plant Stress Responses and Tolerance
- Vitamin C and Antioxidants Research
- Free Radicals and Antioxidants
- Amino Acid Enzymes and Metabolism
- Plant Molecular Biology Research
- Polyamine Metabolism and Applications
- Mitochondrial Function and Pathology
- Microbial Metabolic Engineering and Bioproduction
- Plant Pathogenic Bacteria Studies
- Endoplasmic Reticulum Stress and Disease
- Plant-Microbe Interactions and Immunity
- Legume Nitrogen Fixing Symbiosis
- Antioxidant Activity and Oxidative Stress
- Protein Structure and Dynamics
- Advanced Proteomics Techniques and Applications
- Heat shock proteins research
- Plant responses to water stress
- Enzyme function and inhibition
- Evolution and Genetic Dynamics
- Cannabis and Cannabinoid Research
- Lipid metabolism and biosynthesis
- Mast cells and histamine
Instituto de Hortofruticultura Subtropical y Mediterránea "La Mayora"
2018-2024
Universidad de Málaga
2003-2024
Consejo Superior de Investigaciones Científicas
2015-2024
Instituto de Biotecnología de León
1998
Laboratoire Physiologie Cellulaire & Végétale
1987
Eukaryotic endoplasmic reticulum (ER)-plasma membrane (PM) contact sites are evolutionarily conserved microdomains that have important roles in specialized metabolic functions such as ER-PM communication, lipid homeostasis, and Ca2+ influx. Despite recent advances knowledge about site components yeast (Saccharomyces cerevisiae) mammals, relatively little is known the functional significance of these structures plants. In this report, we characterize Arabidopsis (Arabidopsis thaliana)...
Abstract Endoplasmic reticulum–plasma membrane contact sites (ER–PM CS) play fundamental roles in all eukaryotic cells. Arabidopsis thaliana mutants lacking the ER–PM protein tether synaptotagmin1 (SYT1) exhibit decreased PM integrity under multiple abiotic stresses, such as freezing, high salt, osmotic stress, and mechanical damage. Here, we show that, together with SYT1, stress-induced SYT3 is an that also functions maintaining integrity. The CS localization of SYT1 dependent on...
Abstract The enzymes involved in l-ascorbate biosynthesis photosynthetic organisms (the Smirnoff–Wheeler [SW] pathway) are well established. Here, we analyzed their subcellular localizations and potential physical interactions assessed role the control of ascorbate synthesis. Transient expression C terminal-tagged fusions SW genes Nicotiana benthamiana Arabidopsis thaliana mutants complemented with genomic constructs showed that while GDP-d-mannose epimerase is cytosolic, all from...
Brassinosteroids (BRs) form a group of steroidal hormones essential for plant growth, development, and stress responses. BRs are perceived extracellularly by plasma membrane receptor-like kinases that activate an interconnected signal transduction cascade, leading to the transcriptional regulation BR-responsive genes. TETRATRICOPEPTIDE THIOREDOXIN-LIKE (TTL) genes specific land plants, their encoded proteins defined presence protein–protein interaction motives, is, intrinsic disordered...
TETRATRICOPEPTIDE THIOREDOXIN-LIKE (TTL) proteins are characterized by the presence of six tetratricopeptide repeats in conserved positions and a carboxyl-terminal region known as thioredoxin-like domain with homology to thioredoxins. In Arabidopsis (Arabidopsis thaliana), TTL gene family is composed four members, founder member, TTL1, required for osmotic stress tolerance. Analysis sequenced genomes indicates that genes specific land plants. this study, we report expression profiles using...
The strong negative correlation between glycolytic flux and intracellular ATP concentration observed in yeast has long been an intriguing counterintuitive phenomenon, which referred to as the paradox. Herein, using principles of irreversible thermodynamics it was shown that if ATP-consuming pathways are more sensitive extracellular glucose than glycolysis, then upon addition glycolysis performance can switch from efficient working regime a dissipative regime, vice versa, depending on...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTGlycolysis in Wonderland: The Importance of Energy Dissipation Metabolic PathwaysJ. Carlos Aledo and Alicia Esteban del Valle View Author Information Departamento de Biología Molecular y Bioquímica, Facultad Ciencias, Universidad Málaga, 29071 SpainCite this: J. Chem. Educ. 2002, 79, 11, 1336Publication Date (Web):November 1, 2002Publication History Received3 August 2009Published online1 November 2002Published inissue 1...
ABSTRACT Endoplasmic Reticulum-Plasma Membrane contact sites (ER-PM CS) are evolutionarily conserved membrane domains found in all eukaryotes, where the endoplasmic reticulum (ER) closely interfaces with plasma (PM). This short distance, typically 10-30 nm, is achieved Arabidopsis through action of tether proteins such as Synaptotagmins (SYTs). comprises five SYT members ( SYT1-SYT5 ), but whether they possess overlapping or distinct biological functions remains elusive. SYT1...
Abstract Despite the utility that energy diagrams have as a teaching and learning tool, survey of their use, in seven popular Biochemistry textbooks, reveals there is certain confusion around this topic. In our opinion, arises from reluctance authors to consider indicate conditions under which reaction being represented occurs. For an enzyme‐catalyzed reaction, it should be stressed that, where overall spontaneous, each elementary step must exhibit negative free change, properly reflected...
Brassinosteroids (BRs) play key roles in diverse plant growth processes through a complex signaling pathway. Components orchestrating the BR pathway include receptors such as kinases, transcription factors, protein kinases and phosphatases. The proper functioning of receptor kinase BRI1 factors BES1/BZR1 depends on their dephosphorylation by type 2A phosphatases (PP2A). In this work, we report that an additional phosphatase family, one (PP1), contributes to regulation Co-immunoprecipitation...
SUMMARY Endoplasmic Reticulum-Plasma Membrane contact sites (ER-PM CS) play fundamental roles in all eukaryotic cells. Arabidopsis mutants lacking the ER-PM protein tether synaptotagmin1 (SYT1) exhibit decreased plasma membrane (PM) integrity under multiple abiotic stresses such as freezing, high salt, osmotic stress and mechanical damage. Here, we show that, together with SYT1 , stress-induced SYT3 is an that also functions maintaining PM integrity. The CS localization of dependent on...
Download This Paper Open PDF in Browser Add to My Library Share: Permalink Using these links will ensure access this page indefinitely Copy URL DOI
Endoplasmic Reticulum-Plasma Membrane contact sites (ER-PM CS) are evolutionarily conserved membrane domains found in all eukaryotes, where the endoplasmic reticulum (ER) closely interfaces with plasma (PM). This short distance is achieved plants through action of tether proteins such as Synaptotagmins (SYTs). Arabidopsis comprises five SYT members ( SYT1-SYT5 ), but whether they possess overlapping or distinct biological functions remains elusive. SYT1 , best-characterized member, plays...
Endoplasmic reticulum-plasma membrane contact sites (ER-PM CSs) are evolutionarily conserved domains found in all eukaryotes, where the ER closely interfaces with PM. This short distance is achieved plants through action of tether proteins such as synaptotagmins (SYTs). Arabidopsis comprises five SYT members (SYT1-SYT5), but whether they possess overlapping or distinct biological functions remains elusive. SYT1, best-characterized member, plays an essential role resistance to abiotic stress....
Abstract Brassinosteroids (BRs) form a group of steroidal hormones essential for plant growth, development and stress responses. Here, we report that plant-specific TETRATRICOPEPTIDE THIOREDOXIN-LIKE (TTL) proteins are positive regulators BR signaling functioning as scaffold components in Arabidopsis. TTL3 forms complex with all core involved signaling, including the receptor kinase BRASSINOSTEROID INSENSITIVE1 (BRI1), transcription factor BRASSINAZOLE RESISTANT1 (BZR1) phosphatase...