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MIPs and Their Roles in the Exchange of Metalloids (Hardcover, Edition.)
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MIPs and Their Roles in the Exchange of Metalloids (Hardcover, Edition.)
Series: Advances in Experimental Medicine and Biology, 679
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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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