MIPs and Their Roles in the Exchange of Metalloids
Sixteen years have passed since human aquaporin-1 (AQP1) was discovered as the first water channel, facilitating trans-membrane water fluxes. Subsequent years of research showed that the water channel AQP1 was only the tip of an iceberg; the iceberg itself being the ubiquitous super family of membrane intrinsic proteins (MIPs) that facilitate trans-membrane transport of water and an increasing number of small, water-soluble and uncharged compounds. Here we introduce you to the superfamily of MIPs and provide a summary about our gradually refined understanding of the phylogenetic relationship of its members. This volume is dedicated to the metalloids, a recently discovered group of substrates for a number of specific MIPs in a diverse spectrum of organisms. Particular focus is given to the essential boron, the beneficial silicon and the highly toxic arsenic. The respective MIP isoforms that facilitate the transport of these metalloids include members from several clades of the phylogenetic tree, suggesting that metalloid transport is an ancient function within this family of channel proteins. Among all the various substrates that have been shown to be transported by MIPs, metalloids take an outstanding position. While water transport seems to be a common function of many MIPs, single isoforms in plants have been identified as being crucially important for the uptake of boric acid as well as silicic acid. Here, the function seems not to be redundant, as mutations in those genes render plants deficient in boron and silicon, respectively.
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A Family of Highly Regulated Multifunctional Channels
Chapter 2 Phylogeny of Major Intrinsic Proteins
Chapter 3 Metalloids Soil Chemistry and the Environment
Chapter 4 Arsenic Transport in Prokaryotes and Eukaryotic Microbes
Consequences in the Treatment of Human Diseases
Chapter 6 Roles of Vertebrate Aquaglyceroporins in Arsenic Transport and Detoxification
Autres éditions - Tout afficher
Acad Sci USA accumulation activity analysis antimony AQP1 AQP3 AQP9 AQPs aquaglyceroporins aquaporin Arabidopsis thaliana arsenic arsenite As(III As(V Bienert bilayer Biol Chem biomimetic biomimetic membrane BOR1 boric acid boron cell wall cerevisiae channel proteins coli compounds concentration detoxification drug efflux transporter endodermis environment Escherichia coli expression Fps1p function gene GlpF glycerol homologs human influx inhibition inorganic isoforms Leishmania lipid LmAQP1 Lsi1 Lsi2 maize major intrinsic protein mechanism membrane protein metabolism metalloid transport metalloids methylated MIPs MMA(III molecular molecules mutant Natl Acad Sci NIPs oocytes OsLsi1 osmotic oxidation pathway phosphate transporters phosphorylation phylogenetic physiological Plant Cell Plant Physiol plasma membrane pore Proc Natl Acad regulation residues RG-II rice role roots Rosen BP Saccharomyces cerevisiae Sb(III sequences silicic acid silicon soil solution speciation species Springer Science+Business Media structure subfamilies substrate tissues toxicity translocation transmembrane uptake water channel water permeability wild type Xenopus oocytes xylem Yamaji yeast