Javier Valdez Taubas

ORCID: 0000-0002-2806-9419
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About
Contact & Profiles
Research Areas
  • Cellular transport and secretion
  • Fungal and yeast genetics research
  • Endoplasmic Reticulum Stress and Disease
  • Protein Kinase Regulation and GTPase Signaling
  • Lipid Membrane Structure and Behavior
  • Enzyme Structure and Function
  • Peptidase Inhibition and Analysis
  • Glycosylation and Glycoproteins Research
  • Protein Structure and Dynamics
  • Ubiquitin and proteasome pathways
  • Nanocluster Synthesis and Applications
  • Autophagy in Disease and Therapy
  • Trace Elements in Health
  • Amino Acid Enzymes and Metabolism
  • Studies on Chitinases and Chitosanases
  • Diabetes Treatment and Management
  • Caveolin-1 and cellular processes
  • Lipid metabolism and biosynthesis
  • Machine Learning in Bioinformatics
  • Inflammatory mediators and NSAID effects
  • Parasites and Host Interactions
  • Drug Transport and Resistance Mechanisms
  • Lipoproteins and Cardiovascular Health
  • Insect Resistance and Genetics
  • Fungal Infections and Studies

Research Centre in Biological Chemistry of Córdoba
2003-2023

Consejo Nacional de Investigaciones Científicas y Técnicas
2003-2023

Universidad Nacional de Córdoba
2008-2023

MRC Laboratory of Molecular Biology
2003-2007

It is still unclear why some proteins that travel along the secretory pathway are retained in Golgi complex while others follow their way to plasma membrane (PM). Recent bioinformatic analyses on a large number of single spanning support hypothesis specific features Trans-Membrane Domain (TMD) relevant sorting these particular organelles. Here we experimentally test this for and PM proteins. Using SNARE Sft1 Sso1 from Saccharomyces cerevisiae as model proteins, modified length TMDs volume...

10.1242/jcs.130658 article EN Journal of Cell Science 2013-01-01

S-acylation (commonly known as palmitoylation) is a widespread post-translational modification that consists of the addition lipid molecule to cysteine residues protein through thioester bond. This predominantly mediated by family proteins referred PATs (palmitoyltransferases). Most are polytopic membrane proteins, with four six transmembrane domains, conserved DHHC motif and variable C-and N-terminal regions, probably responsible for conferring localization substrate specificity. There very...

10.1042/bj20080921 article EN Biochemical Journal 2009-01-13

Slc11a1 (formerly Nramp1) is a proton/divalent cation transporter that regulates homeostasis in macrophages. Slc11a2 mediates divalent uptake via the gut and delivery into cells. The mode of action two transporters remains controversial. Heterologous expression frog oocytes shows symporter, whereas an antiporter fluxing cations against proton gradient. This explains why Slc11a2, but not Slc11a1, can complement EGTA sensitivity smf1Delta/smf2Delta/smf3Delta yeast. However, some studies...

10.1074/jbc.m707057200 article EN cc-by Journal of Biological Chemistry 2007-10-12

S-acylation, commonly known as palmitoylation, is a widespread post-translational modification of proteins that consists the thioesterification one or more cysteine residues with fatty acids. This catalysed by family PATs (palmitoyltransferases), characterized presence 50-residue long DHHC-CRD (Asp-His-His-Cys cysteine-rich domain). To gain knowledge on structure-function relationships these proteins, we carried out random-mutagenesis assay designed to uncover essential amino acids in Swf1,...

10.1042/bj20121693 article EN Biochemical Journal 2013-06-25

Many proteins are modified after their synthesis, by the addition of a lipid molecule to one or more cysteine residues, through thioester bond. This modification is called S-acylation, and commonly palmitoylation. reaction carried out family enzymes, palmitoyltransferases (PATs), characterized presence conserved 50- aminoacids domain "Asp-His-His-Cys- Cysteine Rich Domain" (DHHC-CRD). There 7 members this in yeast Saccharomyces cerevisiae, each these thought be responsible for palmitoylation...

10.1371/journal.pone.0016969 article EN cc-by PLoS ONE 2011-02-24

Protein S-acyltransferases, also known as palmitoyltransferases (PATs), are characterized by the presence of a 50-amino acid domain called DHHC domain. Within this domain, these four amino acids constitute highly conserved motif. It has been proposed that palmitoylation reaction occurs through palmitoyl-PAT covalent intermediate involves cysteine in Mutation results lack function for several PATs, and DHHA or DHHS mutants used regularly catalytically inactive controls. In genetic screen to...

10.1074/jbc.m115.651356 article EN cc-by Journal of Biological Chemistry 2015-07-30

GalT2 (UDP-Gal:GA2/GM2/GD2 β-1,3-galactosyltransferase) is a Golgi-resident type II membrane protein that participates in the synthesis of glycosphingolipids. The molecular determinants for traffic and localization this other glycosyltransferases are still poorly characterized. Considering possibility interactions with proteins may influence these processes, present study we carried out yeast two-hybrid screening using elements N-terminal domain as bait. In screening, identified calsenilin...

10.1042/bj20071725 article EN Biochemical Journal 2008-04-25

A superfamily of proteins called cysteine transmembrane is widely distributed across eukaryotes. These small are characterized by the presence a conserved motif at C-terminal region, rich in cysteines, that has been annotated as domain. Orthologs these have involved resistance to pathogens and metal detoxification. The yeast members family YBR016W, YDL012C, YDR034W-B, YDR210W. Here, we begin characterization molecular level show Ybr016w, Ydr034w-b, Ydr210w palmitoylated proteins. Protein...

10.1016/j.jbc.2023.105609 article EN cc-by-nc-nd Journal of Biological Chemistry 2023-12-28

Abstract Yeast exomer is a heterotetrameric complex that assembled at the trans-Golgi network, which required for delivery of distinct set proteins to plasma membrane using ChAPs (Chs5-Arf1 binding proteins) Chs6 and Bch2 as dedicated cargo adaptors. However, our results show significant functional divergence between them, suggesting an evolutionary specialization among ChAPs. Moreover, characterization mutants in several fungi indicates exomer’s function adaptor late acquisition associated...

10.1534/genetics.118.300767 article EN Genetics 2018-02-06

The molecular mechanisms underlying the ERα nuclear/cytoplasmic pool that modulates pituitary cell proliferation have been widely described, but it is still not clear how targeted to plasma membrane. aim of this study was analyse palmitoylation and membrane (mERα) pool, their participation in E2-triggered membrane-initiated signalling normal tumour growth. Cell cultures were prepared from anterior pituitaries female Wistar rats GH3 cells, treated with 10 nM oestradiol (E2). basal expression...

10.1530/joe-18-0418 article EN Journal of Endocrinology 2018-11-01

Protein S-acylation or palmitoylation is a widespread post-translational modification that consists of the addition lipid molecule to cysteine residues proteins through thioester bond. Palmitoylation and palmitoyltransferases (PATs) have been linked several types cancers, diseases central nervous system many infectious where pathogens use host cell machinery palmitoylate their effectors. Despite importance in physiology disease, progress field has hampered by lack potent-specific inhibitors...

10.1098/rsob.200415 article EN cc-by Open Biology 2021-08-01

Ganglioside glycosyltransferases (GGTs) are type II membrane proteins bearing a short N-terminal cytoplasmic tail, transmembrane domain (TMD), and lumenal catalytic domain. The expression activity of these enzymes largely determine the quality glycolipids that decorate mammalian cell membranes. Many (GTs) themselves glycosylated, this is important for their proper localisation, but few if any other post-translational modifications have been reported. Here, we show GGTs, ST3Gal-V, ST8Sia-I,...

10.1042/bcj20170124 article EN Biochemical Journal 2017-07-12

Endocytosis is crucial for all cells as it allows them to incorporate material from the extracellular space and control availability of transmembrane proteins at plasma membrane. In yeast, endocytosis followed by recycling membrane results in a polarised distribution kinetic mechanism. Here, we report that increasing volume residues constitute exoplasmic half domain (TMD) yeast SNARE Sso1, type II protein, its Expression this chimera strains affected either or revealed polarisation achieved...

10.1242/jcs.202937 article EN Journal of Cell Science 2017-11-15
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