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While the role of many of these transporter is unknown, in some
cases, these transporters appear to be involved in the K+
uptake that drives cell expansion and plant development. If these
proteins function in the plasma and vacuolar membranes, they may be
involved in uptake into the cell and remobilization from the
vacuole. Recent evidence suggests that at least one rice KUP is
localized to the vacuolar membrane.
In plants very little is
know about how KUP transporters function precisely. For some of the
transporters in Arabidopsis, barley and cyanobacteria the kinetics
and selectivity have been studied. Some of the plant KUPs have been
shown to have a dual affinity for potassium and others had some
permeability to Na+ as well as K+.
Characterization of two
Arabidopsis mutants in KUP genes has revealed that they play
a role in cell expansion. The tiny root hairs (trh1) mutant
has a defect in root hair elongation and is a null allele of KUP4.
The shy3-1 mutant has a dwarf phenotype due to decreased cell
expansion in several tissues as a result of a missense mutation in
the KUP2 gene. These results highlight the importance of
these two KUP transporters in plant development. Another report also
suggests that KUP transporter expression is correlated with the
development and elongation of one of the largest single cells in the
plant kingdom: the cotton fiber.
Bacteria (click
for published references)
The KUP (TrkD) protein has been identified in E. coli and
homologues exist in both Gram-positive and Gram-negative bacteria.
In E. coli KUP mediates low affinity K+ uptake. It
has been suggested that the E. coli KUP protein is a secondary
transporter. Uptake is blocked by protonophores such as CCCP and
there is evidence for a proton symport mechanism.
Yeast (click
for published references)
The KUP transporter system in Schwanniomyces occidentalis has
been shown to function as a high affinity (20 µM) K+
uptake transporter. In Neurospora crassa the genes encoding
KUPs have been cloned and the K+ uptake system encoded by
KUP was shown to be a high affinity K+:H+
symporter. |