MINIREVIEW

Potassium channels in plant cells

Ingo Dreyer1 and Nobuyuki Uozumi2
1 Plant Biophysics and Heisenberg Group of Biophysics and Molecular Plant Biology, Centro de Biotecnologia y Genomica de Plantas,
Universidad Politécnica de Madrid, Spain
2 Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University, Japan

Keywords Potassium (K+) is the most abundant inorganic cation in plant cells.
Arabidopsis thaliana; K+ channel; Unlike animals, plants lack sodium ⁄ potassium exchangers. Instead, plant
tetramerization; voltage sensor
cells have developed unique transport systems for K+ accumulation and
release. An essential role in potassium uptake and efflux is played by potas-
Correspondence
I. Dreyer, Centro de Biotecnologia y sium channels. Since the first molecular characterization of K+ channels
Genomica de Plantas, Universidad from Arabidopsis thaliana in 1992, a large number of studies on plant
Politécnica de Madrid, Campus de potassium channels have been conducted. Potassium channels are consid-
Montegancedo, Carretera M-40, km 37.7, ered to be one of the best characterized class of membrane proteins in
28223-Pozuelo de Alarcón (Madrid), Spain plants. Nevertheless, knowledge on plant potassium channels is still incom-
Fax: +34 91 715 7721
plete. This minireview focuses on recent developments in the research of
Tel: +34 91 336 4588
potassium transport in plants with a strong focus on voltage-gated potas-
E-mail: ingo.dreyer@upm.es
N. Uozumi, Department of Biomolecular sium channels.
Engineering, Graduate School of
Engineering, Tohoku University, Aobayama
6-6-07, Sendai 980-8579, Japan
Fax: +81 22 795 7293
Tel: +81 22 795 7280
E-mail: uozumi@biophy.che.tohoku.ac.jp

(Received 28 April 2011, revised 26 August

2011, accepted 21 September 2011)

doi:10.1111/j.1742-4658.2011.08371.x

Introduction
The essential mineral nutrient potassium (K+) is the
predominant inorganic ion of plant cells where it can
contribute up to 10% of the dry mass [1]. K+ is recog-
nized as a rate-limiting factor for crop yield and
quality. It plays a major role as stabilizer in metabo-
lism and as an osmoticum contributing to cellular
hydrostatic (turgor) pressure, growth and responses to
environmental changes. A high and relatively stable
potassium concentration in certain cell compartments
is important for enzyme activation, stabilization of
protein synthesis, neutralization of negative charges on
proteins, formation of membrane potential in coopera-
tion with the proton motive force, and maintenance of
cytosolic pH homeostasis [2]. The optimal potassium
concentration for enzyme activation and protein syn-
thesis is in the range of 100 mm [3]. This means that
for an optimal metabolic activity of a plant cell, a con-
trolled K+ concentration of about 100 mm has to be

Abbreviations
ABA, abscisic acid; CBL, calcineurin B-like protein; CDPK, calcium-dependent protein kinases; CIPK, CBL-interacting protein kinase;
ER, endoplasmic reticulum; HKT, high affinity K+ uptake transporter; ROS, reactive oxygen species.

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Potassium channels in plants
maintained in metabolically active compartments (such
as for example cytosol, nucleus, stroma of the cholo-
roplast, and in the matrix of mitochondria). Besides
their stabilizing function also the high mobility of K+
ions is used by plants, especially in osmotic phenom-
ena. K+ is the major cationic osmoticum in turgor-dri-
ven processes, e.g. stomatal movement, phototropism,
gravitropism and cell elongation. These few examples
(reviewed in [4–7]) may illustrate that potassium
homeostasis (the maintenance of a dynamic equilib-
rium in the K+ concentration) is of central importance
for plants. The potassium concentration in normal soil
(10–100 lm) is about 3–4 orders of magnitude lower
than in the plant. Therefore a plant has to invest
energy for the uptake of K+ and its transport
throughout the plant. Pioneering work by Epstein
et al. [8] has indicated that K+ uptake from soil into
plant cells is mediated by low and high affinity trans-
port systems taking advantage of the electrical gradient
and ⁄ or the proton motive force established by H+-
ATPases. During the last two decades a variety of
potassium-permeable transmembrane transport systems
– potentially underlying these two components – were
identified at the molecular level; among them are
HKT ⁄ Ktr ⁄ Trk and KT ⁄ HAK ⁄ KUP transporters but
also others (see below) and potassium channels.
High affinity K+ uptake – not just
transporters can do the job
As a high affinity K+ uptake transporter, HKT was
identified in 1994 from a wheat cDNA library [9].
HKT ⁄ Ktr ⁄ Trk transporters and K+ channels in plants
share interesting structural similarities that were
reviewed and explained in more detail recently [10,11].
Nevertheless, despite these similarities the two classes
also differ at crucial positions clearly discriminating
HKT ⁄ Ktr ⁄ Trk from being channels [12–14]. In gen-
eral, proteins of the HKT type function as alkali
cation transport systems linking cytosolic osmotic
homeostasis with salinity tolerance ⁄ toxicity [15–19].
The genome of Arabidopsis thaliana, for instance,
contains a single copy of an HKT ⁄ Ktr ⁄ Trk gene
(AtHKT1;1). It is expressed in the plasma membrane
of xylem parenchyma cells and is proposed to be
involved in extracting sodium ions from xylem vessels
and thus enhances salt tolerance [20–23]. This
re-absorption concept for HKT-mediated salt toler-
ance, however, may be only one aspect of a more com-
plex picture. In barley, expression of the K+ ⁄ Na+
transporter HvHKT2;1 is upregulated by low K+; and
overexpression of HvHKT2;1 led to enhanced Na+
uptake, higher Na+ concentrations in the xylem sap
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I. Dreyer and N. Uozumi
and enhanced translocation of Na+ to leaves. These
responses were correlated with increased barley salt
tolerance [24]. Thus, high affinity K+ transporters of
the HKT type also contribute essentially to Na+ trans-
port and thus contribute to general cation homeostasis
in plants.
Besides transporters of the HKT ⁄ Ktr ⁄ Trk type also
those of the KT ⁄ HAK ⁄ KUP type were proposed to be
the molecular entities of the high affinity K+ uptake
component [25,26]. In particular, AtHAK5 is recog-
nized as a high affinity transporter, being efficient even
at K+ concentrations lower than 10 lm [27]. Addition-
ally, some other transporter types were correlated with
K+ transport activity as well. For instance, some
members of the family of Na+ ⁄ H+ antiporters
(NHXs) and cation ⁄ H+ antiporters (CHXs) possess
K+ transport activity into and out of the cell, which
probably contributes to their function in physiological
conditions [28–30].
The molecular identification of K+ transporting
proteins allowed them to be assigned to the high and
low affinity uptake components experimentally
observed in plants. Transporters certainly contribute to
the high affinity K+ uptake component, whereas K+
channels definitely underlie the low affinity component.
However, this strict separation cannot be generalized.
Channels may contribute to the high affinity K+
uptake component as well.
K+ channels – astonishingly versatile
Potassium channels in plants can be subdivided into
two channel classes: non-voltage-gated and voltage-
gated K+ channels. The genome of the model plant
A. thaliana, for instance, contains 15 genes that encode
subunits of potassium channels (Table 1). The group
of non-voltage-gated K+ channels consists of six mem-
bers, five tandem-pore channels (TPK1–TPK5) and a
single subunit (KCO3) that resulted from gene duplica-
tion of a tandem-pore channel gene and subsequent
partial deletion [31]. TPKs are proposed to assemble
as dimers to form a functional channel [32]. A mono-
meric TPK subunit is characterized by a tandem repeat
structure of ‘transmembrane–pore–transmembrane’ which
resembles the basic motif of a simple K+ channel
subunit. Non-voltage-gated K+ channels have been
reported to be targeted to the tonoplast or other orga-
nelle membranes, except for TPK4 homomers that also
reach the plasma membrane [33–37]. In comparison,
voltage-gated K+ channels are exclusively found at the
plasma membrane (Fig. 1). The family of voltage-gated
(Shaker-like) K+ channels consists of nine members in
Arabidopsis. The proteins show a common structure,
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I. Dreyer and N. Uozumi Potassium channels in plants

Table 1. K+ channels in Arabidopsis. outward-rectifying (Kout) channel subunits, first mem-

Other names
ber cloned in 1998 [48,49]. Kin channels mediate K+
Channel in the literature uptake, Kout channels K+ release, and Ksilent channels
Channel class Sub-family name Locus and databases modify properties of some Kin channels (see below).
Kweak channels have special gating properties that have
Voltage-gated Kin KAT1 AT5G46240
been investigated in detail in the last few years (see
K+ channels KAT2 AT4G18290
AKT1 AT2G26650
below). Due to their diverse functionalities, voltage-
AKT5 AT4G32500 gated K+ channels mediate the uptake of K+ from
SPIK AT2G25600 AKT6 the soil and also essentially contribute to the influx
Ksilent AtKC1 AT4G32650 AtLKT1, and efflux transport processes that are necessary for
KAT3, KC1 the distribution of K+ in the entire plant.
Kweak AKT2 AT4G22200 AKT3, In the following, we focus on selected aspects of
AKT2 ⁄ 3
recent developments in plant potassium channel
Kout SKOR AT3G02850
GORK AT5G37500
research. For overviews on further aspects (e.g. regula-
Voltage- Tandem-pore TPK1 AT5G55630 KCO1 tion by protons, nucleotides, external Ca2+, phosphoi-
independent K+ channels TPK2 AT5G46370 KCO2 nositides, beta subunits and 14-3-3 proteins) and on
K+ channels TPK3 AT4G18160 KCO6 earlier work, we refer to other excellent reviews
TPK4 AT1G02510 KCO4 [11,23,31,39,50–55].
TPK5 AT4G01840 KCO5
KCO3 AT5G46360
Beyond just being doorman – surprising
facets of the K+ selectivity filter
A unique fingerprint of potassium channels of all king-
doms of life is the highly conserved selectivity filter
comprising the characteristic amino acid motif
TxGYGD in the pore loops. This pore allows the pas-
sage of K+ ions across the membrane by stripping off
the hydration shell and replacing it by polar oxygen
atoms of the polypeptide backbone [56]. The geometry
of the selectivity filter is optimally adapted for K+
whereas the passage of other cations such as Na+, for
example, is inhibited. Many studies also on plant K+
channels showed that mutations in the selectivity filter
Fig. 1. Representative possible regulations of K+ channels in the can fundamentally alter the permeation properties of
plasma membrane and organelle membranes in plant cells. the channels [57–59]. The broadest approaches in this
context were launched for the Arabidopsis K+
channels KAT1 and AKT1. For both, libraries of
with six transmembrane domains and one pore loop channels with randomly mutated selectivity filters were
(6TM1P). The first four transmembrane domains fold generated and screened in the yeast Saccharomyces
into the voltage sensor module, and the pore loop cerevisiae [60–62]. Lately, a KAT1 mutant library was
together with the fifth and sixth transmembrane re-inspected and over 200 point mutants in the pore
domains establishes the permeation pathway module. region were examined in S. cerevisiae and Xenopus
Four of these subunits must assemble to form a chan- oocytes to assess the effect of the mutations on ion
nel, with all four pore regions contributing to the for- selectivity. The results indicate that the entire pore of
mation of the central inside layer of the pore and the KAT1 contributes to the ion selectivity of this channel.
selectivity filter [38]. The family of Shaker-like K+ Surprisingly, the study also identified mutations that
channels is the best characterized transporter class in confer enhanced selectivity of K+ over Na+. The cost
plants [39]. At the functional level it subdivides into of this apparent advantage, however, appears to be
four functional subgroups: (a) inward-rectifying (Kin) an increased sensitivity to competing ions such as
channels, first members cloned in 1992 [40–43]; (b) Cs+, for instance. It might thus be speculated that
silent (Ksilent) channel subunits, reported in 1997 for plant K+ channel pores have evolved to balance not
the first time [44,45]; (c) weakly rectifying (Kweak) only K+ ⁄ Na+ selectivity but selectivity over a wide
channels, first member cloned in 1995 [46,47]; and (d) spectrum of potential competing ions [63]. Indeed, the

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Potassium channels in plants
conclusions drawn from KAT1 mutagenesis studies
have physiological implications. Recently, a KAT1-like
channel from melon with unusual K+ ⁄ Na+ perme-
ation ⁄ blocking properties was reported [64]. These
results indicate that even slight differences in the pore
structure may result in an important functional
flexibility.
Geiger et al. [65] presented an illustrative example of
this flexibility by pointing to a mechanism that con-
tributes to an efficient regulation of plant K+ uptake
channels in order to avoid K+ leakage under unfavor-
able conditions, a phenomenon well described before
in vivo [66]. The K+ channel KAT1 is expressed in
guard cells and faces there fluctuations of external K+
in the millimolar range, whereas AKT1, expressed in
root epidermis cells, is usually challenged by much
lower potassium concentrations. The different expres-
sion of the two channels mirrors with distinct func-
tional features of the channel pores. Generally, the
pore of potassium channels undergoes conformational
changes (collapses) upon lowering the extracellular K+
concentration, effectively resulting in channel inactiva-
tion. The critical K+ concentration, below which chan-
nel inactivation occurs, differs between channels
[65,67,68]. While KAT1 exhibits considerable channel
activity down to micromolar K+ concentrations [67],
AKT1 is largely inactivated under these conditions
[65]. The different affinities of the KAT1 and AKT1
pores have fundamental physiological implications.
Upon K+ depletion, channel-mediated K+ efflux, i.e.
K+ leakage from the cell, is reduced in the case of
AKT1 compared with KAT1. Nevertheless, despite the
fact that the K+ (absence) sensor of AKT1 reduces
K+ efflux, it cannot completely prevent K+ loss.
Plants have therefore evolved a second level of K+
efflux control.
A voltage-dependent K+ channel is a tetrameric
protein that can be formed by identical subunits but
also by different subunits [44,69]. Recently, the exis-
tence of heteromeric K+ channels could unequivocally
be proven in vivo [70], and in some cases heteromeric
assembly of plant Shaker-like channel subunits is even
preferred over homomeric assembly [71–73]. In Arabid-
opsis root cells, AKT1 channel subunits assemble with
AtKC1 subunits. The pore of this root K+ channel
complex exhibits a further enhanced sensitivity to low
external K+, being more efficient in preventing K+
loss than AKT1 homomers [65]. It is tempting to spec-
ulate whether the AtKC1 subunit inherits this feature
also for heteromeric channels with other inward-recti-
fying K+ channel subunits (KAT1, KAT2 and AKT2)
[74]. Apart from modifying the pore topology, the
AtKC1 subunit passes special voltage-dependent
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I. Dreyer and N. Uozumi
properties to the channel complex [44,75,76] and
recruits other proteins that modify channel gating
[77,78]. In combination, all these processes allow root
epidermal cells the uptake of K+ through AKT1 ⁄
AtKC1 complexes, which function as a non-return
valve by avoiding loss of cytosolic K+ toward potas-
sium-depleted soils.
Besides K+ uptake channels, K+ release channels
also make use of a pore-intrinsic K+ sensor. In this
case, the K+ sensor property is more evident because
it is an essential part of the gating machinery of these
channels [38,79–82]. The key feature of the K+ sensi-
tivity in these channels is that increasing K+ outside
acts to suppress channel opening in a voltage-depen-
dent manner. As a result the channels only open at
voltages positive to the K+ equilibrium voltage EK
and so ensure K+ efflux regardless of the extracellular
K+ concentration. This ability to adapt channel gating
to the prevailing K+ concentration outside guarantees
that the channels open only when the driving force for
net K+ flux is directed outward, thus ensuring the K+
efflux needed to drive stomatal closure, for example,
even when extracellular K+ varies over concentrations
from 10 nm to 100 mm [83,84]. The K+ release chan-
nel SKOR serves as a model system to uncover the
molecular entities underlying such gating by K+. It
was shown that the K+ sensor phenomenon is
crucially dependent on the interaction of two sites, one
site comprising the residues DMIxG deep within
the last transmembrane helix of the channel subunit
(the so-called S6 gating domain) and the other site
positioned adjacent to this domain in the pore. The
presence of K+ in the pore has a similar stabilizing
effect to that mentioned above for K+ uptake chan-
nels. In this case, however, cations occupying the
selectivity filter press the pore helix against the S6 gat-
ing domain and prolong channel closure, temporarily
locking the channel in a closed state [80]. Thus, the
same K+-dependent feature of the pore is employed
by K+ uptake and K+ release channels in opposite
ways – K+ uptake channels close when external K+
is low, K+ release channels close when external K+ is
high.
K+ channels as direct targets for
cellular signals
Reactive oxygen species (ROS) are important signals
in every eukaryotic cell. In plants, they are essential
for development, stress signaling and triggering of
defense reactions against pathogens [85]. ROS exert
their function on proteins by chemically modifying a
small subset of amino acids, notably cysteine residues,

I. Dreyer and N. Uozumi
and thereby alter protein structure and activity [86].
ROS are reported to regulate the activities of plant
membrane ion channels [87–90] and recently Garcia-
Mata et al. [91] identified the Kout channel SKOR as a
direct target for the ROS H2O2. H2O2 applied from
the outside rapidly enhances current amplitude and
activation kinetics of SKOR. Interestingly, the effect
of H2O2 strongly depends on membrane depolariza-
tion, consistent with an H2O2-sensitive site on the
SKOR protein that is exposed to the outside when the
channel is in the open conformation. By mutating
the 11 cysteine residues of the SKOR subunit in
diverse combinations, a single residue, Cys168, located
within the S3 a-helix of the voltage sensor complex
was pinpointed to be essential for sensitivity to H2O2.
Molecular modeling of SKOR in the open and closed
conformations revealed that this residue is exposed to
the outside – and therefore accessible to H2O2 – only
when the channel is in the open conformation. Thus,
H2O2 promotes a positive feedback mechanism on
active SKOR channels. Similar results were meanwhile
also obtained for the guard cell expressed Kout channel
GORK (J. Riedelsberger and I. Dreyer, Potsdam ⁄
Madrid, unpublished results) indicating a general role
of ROS acting on plant K+ channels.
K+ channels as power switches
Genomes of higher plants comprise a special gene cod-
ing for a K+ channel subunit (Kweak) with exceptional
gating properties: AKT2 ⁄ 3 in Arabidopsis. When
expressed in Xenopus oocytes or COS cells, AKT2-like
channels display two current components with differ-
ent voltage-dependent properties [92]. One channel
subpopulation showed gating analogous to that of K+
uptake channels opening at voltages more negative
than about )100 mV (gating mode 1); the second
showed little sensitivity to voltages below +100 mV,
with channels being open over the entire physiological
voltage range (gating mode 2). Although they are func-
tional as homotetramers, these subunits also assemble
with K+ uptake channel subunits and confer their rec-
tification properties to the heteromeric channels
[71,93]. Switching between the two gating modes is
under post-translational control. An important role is
played by phosphorylation ⁄ dephosphorylation of two
highly conserved serine residues specific to AKT2-like
channels, one in the linker between the voltage sensor
and the pore module and the other in the linker
between the last transmembrane helix and the cytosolic
C-terminus [94]. Additionally, a highly conserved
lysine residue in the voltage sensor of the channel is
involved in this switching process [95].
FEBS Journal 278 (2011) 4293–4303 ª 2011 The Authors Journal compilation ª 2011 FEBS
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Potassium channels in plants
Gajdanowicz et al. [96] provided new insights into
the physiological significance of this gating mode
switch: toggling AKT2-like channels from mode 1 to
the voltage-independent mode 2 taps a ‘potassium
battery’ that efficiently assists the plasma membrane
H+-ATPase in energizing transmembrane transport
processes. This mechanism is predominantly important
in phloem tissues. There, K+ ions, taken up in source
tissues into the phloem by energy (ATP) consumption
and then circulating in the phloem, serve as decentral-
ized energy storage. This energy source can be
exploited by regulation of AKT2-like channels to
overcome local energy limitations. Regulation of
AKT2-like channels is a complex phenomenon that is
currently under deeper investigation. A previous study
identified a phosphatase of type 2C [97] to interact
with AKT2 and to potentially link the AKT2 phos-
phorylation status to the abscisic acid (ABA) signaling
pathway. However, other regulatory mechanisms also
need to be considered [98].
K+ channels are parts of cellular
networks enabling guard cell volume
control and uptake of potassium from
the soil
Guard cells control stomatal aperture by osmotic
swelling and shrinking in response to environmental
conditions such as drought stress, carbon dioxide con-
centration and light irradiation. The volume change of
guard cells is regulated by fluxes of ions and organic
compounds across the membranes. Voltage-gated K+
channels are deeply involved in guard cell volume reg-
ulation. Stoma opening, for instance, is induced by the
influx of several solutes including K+ and Cl) into
guard cells. Plasma membrane H+-ATPases generate
the proton motive force and establish a negative mem-
brane voltage. This induces opening of inward-rectify-
ing K+ channels allowing the influx of K+ ions. For
stoma closure, in turn, plasma membrane proton
pumps and inward-rectifying K+ uptake channels are
inhibited, and chloride channels and outward-rectifying
K+ release channels are activated. As a consequence,
the turgor pressure of the cells reduces; the cell
shrinks. Setting the status of a guard cell for stomata
opening or closure is achieved by signal transduction
pathways involving multiple protein phosphatases and
kinases [99]. These also affect the activity of K+ chan-
nels. Direct evidence for such regulation was obtained
for the guard cell expressed Kin channel KAT1 from
A. thaliana. KAT1 channel activity was impaired by
calcium-dependent protein kinases (CDPKs) from
Vicia faba guard cells [100] and from soybean [101].
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Potassium channels in plants
Potential residues involved in this KAT1 regulation
have been identified in site-directed mutagenesis studies
using protein kinase C mediated phosphorylation in
Xenopus laevis oocytes [102]. This study took advan-
tage of the similarity of the consensus phosphorylation
motif between CDPKs and calcium-dependent ser-
ine ⁄ threonine kinases of Xenopus oocytes including
protein kinase C. Mimicking the phosphorylated status
by mutating certain residues in the cytosolic C-termi-
nal region of KAT1 decreased the number of active
channels.
KAT1 served also as a model system to show the
effect of calcium-independent ABA-activated AAPK ⁄
ABR kinases from guard cells. An AAPK ⁄ ABR kinase
from V. faba phosphorylated the C-terminal region of
KAT1 in an in vitro kinase assay [103]. One out of 10
members of SNF1-related protein kinase from A. thali-
ana, SnRK2.6, is an ortholog of the AAPK ⁄ ABR
kinase from Vicia fava [104]. Purified SnRK.2.6 was
able to phosphorylate residues in the cytosolic C-termi-
nal region of KAT1. Modification of a targeted residue
by mutagenesis abolished KAT1 activity in oocyte
recordings [105]. These studies indicate that K+
uptake channels (such as KAT1) are down-regulated
by kinases in signaling pathways inducing stomatal
closure.
In another context, e.g. in roots, kinases can up-reg-
ulate K+ uptake channel activity. There, K+ channels
are involved in nutrient acquisition mechanisms. For
instance, the Kin channel AKT1 plays an important
role in the absorption of K+ from the soil. AKT1 was
shown to be phosphorylated and activated by a com-
plex of a calcineurin B like protein 1 (CBL1) or CBL9
and the CBL-interacting protein kinase 23 (CIPK23)
[106,107]. Similar results were reported for a Kin chan-
nel expressed in grape berries under drought stress
[108] pointing to a general role of CIPK ⁄ CBL regula-
tion of plant K+ channels. For the prototype of this
research line, AKT1, it was meanwhile shown that sev-
eral CBLs and CIPKs together with phosphatases of
type 2C (PP2CA) built a phosphorylation ⁄ dephosphor-
ylation network [109,110], the dynamics of which still
needs to be explored.
Recently it was shown that a CBL ⁄ CIPK complex
can influence channel function not only by phosphory-
lation. Held et al. [111] showed that the calcium sensor
CBL4 together with the interacting protein kinase
CIPK6 modulate the plasma membrane targeting of
the Kweak channel AKT2. The kinase domain of
CIPK6 was not important for this process. The
isolated regulatory C-terminal domain of CIPK6 was
sufficient for mediating CBL4-dependent and Ca2+-
dependent channel translocation from the endoplasmic
4298 FEBS Journal 278 (2011) 4293–4303 ª 2011 The Authors Journal compilation ª 2011 FEBS
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I. Dreyer and N. Uozumi
reticulum (ER) membrane to the plasma membrane.
Usually, channel trafficking from the ER to the plasma
membrane depends on diacidic motifs that function as
ER export signals and ⁄ or ER retention signals [112].
Thus, it might be that the CBL ⁄ CIPK complex
attached to the channel Ca2+-dependently exposes a
diacidic motif or covers an ER retention signal to
shuttle AKT2 to the plasma membrane. Similar mech-
anisms were proposed for heteromeric channel com-
plexes that were targeted to the plasma membrane
while the homomers were not [71,75,113,114].
In conclusion we can state that K+ channels are
regulated by a variety of different post-translational
processes and we are just at the very tip of the iceberg
in uncovering these regulatory steps.
Acknowledgements
This work was supported by the Abate Juan Ignacio
Molina Excellence Award of the Comisión Nacional
de Investigación Cientı́fica y Tecnológica de Chile
(CONICYT) and the Alexander von Humboldt Foun-
dation (to I.D.), by grants DR430 ⁄ 5-1, DR430 ⁄ 5-2,
DR430 ⁄ 8-1, and by a Heisenberg fellowship of the
German Science Foundation (Deutsche Forschungs-
gemeinschaft) (to I.D.), and by grants-in-aid for scien-
tific research (22020002 and 22380056 to N.U.) from
the Ministry of Education, Culture, Sports, Science
and Technology, and the Japan Society for the Promo-
tion of Science (to N.U.).
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