The α-kinases TRPM6 and TRPM7, but not eEF-2 kinase, phosphorylate the assembly domain of myosin IIA, IIB and IIC
The α-kinases TRPM6 and TRPM7, but not eEF-2 kinase, phosphorylate the assembly domain of myosin IIA, IIB and IIC
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DOI：
10.1016/j.febslet.2008.07.043
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发表时间：
2008-09-03
期刊：
影响因子：
3.5
通讯作者：
van Leeuwen, Frank N.
中科院分区：
文献类型：
--
作者：
Clark, Kristopher;Middelbeek, Jeroen;van Leeuwen, Frank N.
TRPM 6和TRPM 7编码通道激酶。虽然这些通道共享电生理特性和细胞功能，但TRPM 6和TRPM 7是非冗余基因，这提高了激酶具有不同底物的可能性。在这里，我们证明，TRPM 6和TRPM 7磷酸化的组装结构域的肌球蛋白IIA，IIB和IIC上相同的残基。而肌球蛋白IIA的磷酸化仅限于卷曲螺旋结构域，TRPM 6和TRPM 7也磷酸化肌球蛋白IIB和IIC的非螺旋尾部。TRPM 7不磷酸化真核延伸因子-2（eEF-2），并且肌球蛋白II是eEF-2激酶的不良底物。总之，TRPM 6和TRPM 7共享外源性底物，但不与功能上遥远的α-激酶。
TRPM6 and TRPM7 encode channel-kinases. While these channels share electrophysiological properties and cellular functions, TRPM6 and TRPM7 are non-redundant genes raising the possibility that the kinases have distinct substrates. Here, we demonstrate that TRPM6 and TRPM7 phosphorylate the assembly domain of myosin IIA, IIB and IIC on identical residues. Whereas phosphorylation of myosin IIA is restricted to the coiled-coil domain, TRPM6 and TRPM7 also phosphorylate the non-helical tails of myosin IIB and IIC. TRPM7 does not phosphorylate eukaryotic elongation factor-2 (eEF-2) and myosin II is a poor substrate for eEF-2 kinase. In conclusion, TRPM6 and TRPM7 share exogenous substrates among themselves but not with functionally distant alpha-kinases.