Ca2+ signalling in plant cells: the big network!

Trewavas and Malho (1998)

Ca2+ release and uptake
Ca2+-signalling pathways generally involve changes in the concentration of
[Ca2+]c. These changes can arise from the activation of membrane-associated
transporters channels and pumps or through changes in the affinity of Ca2+
binding proteins (CBPs). Channels and pumps have now been localised in the
plasma membrane, tonoplast and endoplasmic reticulum (ER) and regulate inward
Ca2+ current (Thuleau et al., this issue pp 424427). Ion channels located in the
tonoplast and plasma membrane are believed to be responsible for most of the
Ca2+ inward currents. Data collected during an action potential in Chara, however,
suggests that [Ca2+]c increases arise mainly from internal stores other than the
vacuole [19]. Touch-induced [Ca2+]c transients also originate from internal stores
[20], although here the nuclear envelope may be a primary source (A van der Luit,
MR Knight and AJ Trewavas unpublished data). The second messengers,
inositol(1,4,5)triphosphate (IP3) and cyclic adenosine phosphate ribose (cADP-R)
mobilise Ca2+ release from the internal stores of the vacuole and probably the ER
[10,21].
Ca2+ signaling secara umum mempengaruhi konsentrasi Ca2+ di sitosol.
Perubahan ini bisa menaikan aktivitas dari para transporter, channel dan pumps,
atau juga mengubah affinitas dari Ca2+ binding protein (CBPS). Transporter sudah
diketahui bahwa terletak di membrane plasma, tonoplast, RE(Retikulum
endoplasma). Ion channel yang terletak di membrane plasma dan tonoplast
dipercayai bertanggung jawab terhadap masuknya Ca2+.
Phospholipase C is now the proven enzymatic plant source of IP3 and
diacylglyceride [22], whereas cADP-R is synthesised from NAD [23]. CBPs (soluble
or attached to the cytoskeleton) still lack critical examination in plant cells.
Estimates of the cytosolic buffer capacity for Ca2+ (120 mM) [24] do suggest that
CBPs could play a crucial role in signalling mechanisms. Phosphorylation of CBPs,
subsequently modifying Ca2+ binding, could act to trigger the initial stimulus or
modulate the transduction of the signal or even initiate Ca2+ wave propagation
[6,13]

Calcium channels in higher plants

White (1999)
A channel permeable to Ca2, Mg2 and K has been recorded in swollen thylakoids
from spinach chloroplasts [90]. This channel was activated at membrane potentials
promoting cation movement to the intrathylakoid space. Its unitary conductance at
such voltages was 62 pS with 100 mM K and 21 pS with 5 mM Ca2 as the charge
carrier. The physiological role of this channel may be to provide compensatory
cation movements during light-driven H uptake into thylakoids. Incidentally, Ca2

uptake into intact chloroplasts is stimulated by illumination and is inhibited by

ruthenium red [91]. This is thought to stimulate anabolic metabolism.
A channel permeable to K, Na, Cs and Ca2 has been recorded in the nuclear
envelope of nuclei
from red beet [92]. The unitary conductance of this channel was 110 pS in
symmetrical 150 mM KCl, which was reduced to 15 pS by replacing KCl on one side
with 50 mM CaCl2. Most nucleus-attached patches were quiescent, but excision of
the patch resulted in an immediate activation of the channel.
The channel was activated by membrane hyperpolarisation when the [Ca2] on the
side of the channel originally facing the perinuclear space (the lumen of the nuclear
envelope) approached 1 WM. Increasing the perinuclear [Ca2] shifted the
relationship between channel Po and voltage to more positive voltages, thereby
increasing channel Po at physiological membrane potentials. Channel activity was
unaffected by changes in [Ca2]cyt. The channel was blocked by 1 mM Zn2 when
applied to the cytoplasmic side of the channel, and by 2 mM amiloride when applied
to the side facing the perinuclear space.
Based on the sensitivity of this channel to the [Ca2] of the periplasmic space, a
role for this channel in regulating Ca2-dependent nuclear processes has been
proposed [92].

Calcium uptake mechanisms of mitochondria

Domingo dan demaurex (2010)
The free Ca2+ concentration in plant mitochondria is maintained at
levels as low as less than 100nM, similar to the levelsvof Ca2+ in
the cytosol. Oscillations in the free Ca2+ concentration of
mitochondria have been detected using transgenicplants in which
the aequorin apoprotein (Logan and Knight, 2003) or cameleon
proteins (Loro et al., 2012, 2013) are targeted to mitochondria. Cold
stress, hyperosmotic stress, and touch stimulus evoke transient
Ca2+ signals that last 1020 s, which are distinct from the cytosolic
Ca2+ signals, suggesting that mitochondrial and cytosolic Ca2+
dynamics are differentially regulated (Logan and Knight, 2003). In
contrast to these stresses, hydrogen peroxide treatment results in a
long-lasting (>120 s) increase in mitochondrial Ca2+ concentration.
Recently, it has been reported that osmotic stress and extracellular
ATP induce mitochondrial Ca2+ oscillations, which are different from
cytosolic Ca2+ signals (Loro et al., 2012). Mitochondria seem likely
modulate the mitochondrial Ca2+ signals actively independently of
the cytosolic signals. Furthermore, Manzoor et al. (2012)
demonstrated that

Konsentrasi Ca2+ di dalam mitochondria diatur pada konsentrasi

lebih rendap dari 100 nM, mirip seperti konsentrasi Ca2+ di stiosil.
Masuk keluarnya konsentrasi ca2+ bebas dari mitokondria telah di
deteksi menggunakan transgenic plants dimana aequorin
apoprotein atau camelon protein ditargetkan pada mitokondria.
Stress cold, stress hyper osmotic stress, dan rangsangan sentuhan
membangkitkan sinyal Ca2+ sementara sekitar 10-20s, yang
berbeda dengan sinyal ca2+ di sitosol, menunjukan bahwa
pergerakan ca2+ di mitokondria dan sitosol di regulasi secara
berbeda. Bahkan terhadap perlakuan hydrogen peroxide menghasil
konsentrasi ca2+ yang lama di mitokondria (sekitar >120 detik).
Baru-baru inipun telah dilaporkan bahwa stress osmotic dan ATP
ekstraseluler menginduksi osilasi Ca2+, yang berbeda dengan