B. Gillo et al., COEXPRESSION OF DROSOPHILA TRP AND TRP-LIKE PROTEINS IN XENOPUS OOCYTES RECONSTITUTES CAPACITATIVE CA2+ ENTRY, Proceedings of the National Academy of Sciences of the United Statesof America, 93(24), 1996, pp. 14146-14151
Capacitative Ca2+ entry is a component of the inositol-lipid signaling
in which depletion of inositol 1,4,5-trisphosphate (InsP(3))-sensitiv
e Ca2+ stores activates Ca2+ influx by a mechanism that is still unkno
wn. This pathway plays a central role in cellular signaling, which is
mediated by many hormones, neurotransmitters, and growth factors, Stud
ies of Drosophila photoreceptors provided the first putative capacitat
ive Ca2+ entry mutant designated transient receptor potential (trp) an
d a Drosophila gene encoding TRP-like protein (trpl), It is not clear
how the Ca2+ store depletion signal is relayed to the plasma membrane
and whether both TRP and TRPL participate in this process. We report h
ere that coexpressing Drosophila TRP and TRPL in Xenopus oocytes syner
gistically enhances the endogenous Ca2+-activated Cl- current and prod
uces a divalent inward current, Both of these currents are activated b
y Ca2+ store depletion. In the absence of Ca2+, Mg2+ is the main charg
e carrier of the divalent current, This current is characterized by la
nthanum sensitivity and a voltage-dependent blocking effect of Mg2+, w
hich Is relieved at both hyperpolarizing (inward rectification) and de
polarizing (outward rectification) potentials. The store-operated diva
lent current is neither observed in native oocytes nor in oocytes expr
essing either TRP or TRPL alone, The production of this current implic
ates a cooperative action of TRP and TRPL in the depletion-activated c
urrent.