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首页> 外文期刊>The Journal of biological chemistry >Methionine Sulfoxide Reductase B1 (MsrB1) Recovers TRPM6 Channel Activity during Oxidative Stress
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Methionine Sulfoxide Reductase B1 (MsrB1) Recovers TRPM6 Channel Activity during Oxidative Stress

机译：甲硫氨酸亚砜还原酶B1（MSRB1）在氧化应激期间恢复TRPM6通道活性

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摘要

Mg2+ is an essential ion for many cellular processes, including protein synthesis, nucleic acid stability, and numerous enzymatic reactions. Mg2+ homeostasis in mammals depends on the equilibrium between intestinal absorption, renal excretion, and exchange with bone. The transient receptor potential melastatin type 6 (TRPM6) is an epithelial Mg2+ channel, which is abundantly expressed in the luminal membrane of the renal and intestinal cells. It functions as the gatekeeper of transepithelial Mg2+ transport. Remarkably, TRPM6 combines a Mg2+-permeable channel with an α-kinase domain. Here, by the Ras recruitment system, we identified methionine sulfoxide reductase B1 (MsrB1) as an interacting protein of the TRPM6 α-kinase domain. Importantly, MsrB1 and TRPM6 are both present in the renal Mg2+-transporting distal convoluted tubules. MsrB1 has no effect on TRPM6 channel activity in the normoxic conditions. However, hydrogen peroxide (H2O2) decreased TRPM6 channel activity. Co-expression of MsrB1 with TRPM6 attenuated the inhibitory effect of H2O2 (TRPM6, 67 ± 5% of control; TRPM6 + MsrB1, 81 ± 5% of control). Cell surface biotinylation assays showed that H2O2 treatment does not affect the expression of TRPM6 at the plasma membrane. Next, mutation of Met1755 to Ala in TRPM6 reduced the inhibitory effect of H2O2 on TRPM6 channel activity (TRPM6 M1755A: 84 ± 10% of control), thereby mimicking the action of MsrB1. Thus, these data suggest that MsrB1 recovers TRPM6 channel activity by reducing the oxidation of Met1755 and could, thereby, function as a modulator of TRPM6 during oxidative stress.
机译：Mg2 +是许多细胞过程的基本离子，包括蛋白质合成，核酸稳定性和许多酶促反应。哺乳动物中的Mg2 +稳态取决于肠道吸收，肾脏排泄和骨骼的交换之间的平衡。瞬态受体潜在的素母苷酰型6（TRPM6）是上皮MG2 +通道，其在肾和肠细胞的腔膜中大量表达。它用作TRANSEPETHELIAL MG2 +运输的网守。值得注意的是，TRPM6将MG2 +可-Emermable通道与α-激酶结构域组合。这里，通过Ras募集系统，我们将甲硫氨酸亚砜还原酶B1（MSRB1）鉴定为TRPM6α-激酶结构域的相互作用蛋白质。重要的是，MSRB1和TRPM6都存在于肾MG2 + - 转换远端卷积小管中。 MSRB1对常规条件下的TRPM6信道活动没有影响。然而，过氧化氢（H 2 O 2）降低了TRPM6通道活性。具有TRPM6的MSRB1的共表达抑制了H2O2（TRPM6,67±5％的控制; TRPM6 + MSRB1,81±5％的控制）的抑制作用。细胞表面生物素化测定结果表明，H 2 O 2处理不会影响Trpm6在质膜上的表达。接下来，TRPM6中MAT1755至ALA的突变降低了H2O2对TRPM6通道活性的抑制作用（TRPM6 M1755A：84±10％的控制），从而模仿MSRB1的作用。因此，这些数据表明MSRB1通过减少MAT1755的氧化来恢复TRPM6信道活动，从而可以在氧化应力期间用作TRPM6的调节剂。

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