Control of calcium signal propagation to the mitochondria by inositol 1,4,5-trisphosphate-binding proteins
Control of calcium signal propagation to the mitochondria by inositol 1,4,5-trisphosphate-binding proteins
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DOI:
10.1074/jbc.m411591200
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发表时间:
2005-04-01
影响因子:
4.8
通讯作者:
Hajnóczky, G
中科院分区:
文献类型:
--
作者:
LIn, XN;Várnai, P;Hajnóczky, G
Cytosolic Ca2+ ([Ca2+](c)) signals triggered by many agonists are established through the inositol 1,4,5-trisphosphate (IP3) messenger pathway. This pathway is believed to use Ca2+-dependent local interactions among IP3 receptors (IP3R) and other Ca2+ channels leading to coordinated Ca2+ release from the endoplasmic reticulum throughout the cell and coupling Ca2+ entry and mitochondrial Ca2+ uptake to Ca2+ release. To evaluate the role of IP3 in the local control mechanisms that support the propagation of [Ca2+](c) waves, storeoperated Ca2+ entry, and mitochondrial Ca2+ uptake, we used two IP3-binding proteins (IP3BP): 1) the PH domain of the phospholipase C-like protein, p130 (p130PH); and 2) the ligand-binding domain of the human type-IIP3R (IP3R224-605). As expected, p130PH-GFP and GFP-IP3R224-605 behave as effective mobile cytosolic IP3 buffers. In COS-7 cells, the expression of IP3BPs had no effect on store-operated Ca2+ entry. However, the IP3-linked [Ca2+] c signal appeared as a regenerative wave and IP3BPs slowed down the wave propagation. Most importantly, IP3BPs largely inhibited the mitochondrial [Ca2+] signal and decreased the relationship between the [Ca2+](c) and mitochondrial [Ca2+] signals, indicating disconnection of the mitochondria from the [Ca2+](c) signal. These data suggest that IP3 elevations are important to regulate the local interactions among IP3Rs during propagation of [Ca2+](c) waves and that the IP3-dependent synchronization of Ca2+ release events is crucial for the coupling between Ca2+ release and mitochondrial Ca2+ uptake.