MIPs and Their Roles in the Exchange of MetalloidsThomas P. Jahn, Gerd P. Bienert Springer Science & Business Media, 11 janv. 2011 - 145 pages 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. |
Table des matières
A Family of Highly Regulated Multifunctional Channels | 1 |
Chapter 2 Phylogeny of Major Intrinsic Proteins | 19 |
Chapter 3 Metalloids Soil Chemistry and the Environment | 33 |
Chapter 4 Arsenic Transport in Prokaryotes and Eukaryotic Microbes | 47 |
Consequences in the Treatment of Human Diseases | 57 |
Chapter 6 Roles of Vertebrate Aquaglyceroporins in Arsenic Transport and Detoxification | 71 |
Involvement of Arabidopsis NIP51 and NIP61 | 83 |
Chapter 8 Silicon Transporters in Higher Plants | 98 |
New Players and Their Potential Role | 111 |
Chapter 10 Major Intrinsic Proteins in Biomimetic Membranes | 127 |
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Autres éditions - Tout afficher
MIPs and Their Roles in the Exchange of Metalloids Thomas P. Jahn,Gerd P. Bienert Aucun aperçu disponible - 2010 |
Expressions et termes fréquents
accumulation activity addition analysis antimony AQP1 AQP9 AQPs aquaglyceroporins aquaporin Arabidopsis arsenic arsenite As(III As(V Bangladesh Biol Chem biomimetic BOR1 boric acid boron cell chapter characterization coli compared compounds concentration containing demonstrated drug effects efflux elements environment et al expression facilitate function gene GlpF glycerol groups growth higher human identified important increased inhibition inorganic involved lead Leishmania levels lipid localized Lsi1 maize mechanism metalloids methylated MIPs molecular molecules mutant Nature NIPs observed oocytes organic osmotic pathway permeability phosphate phylogenetic physiological Plant Cell Plant Physiol plants plasma membrane pore potential present processes recent reduced region regulation reported residues resistance response rice role roots Sb(III selectivity sequences showed shown silicon similar soil solution species structure studies subfamilies substrate suggesting thaliana tissues tolerance toxicity transport uptake water channel water permeability