The α-kinases TRPM6 and TRPM7, but not eEF-2 kinase, phosphorylate the assembly domain of myosin IIA, IIB and IIC

被引：68

作者：

Clark, Kristopher ^{[2
]}

Middelbeek, Jeroen ^{[2
]}

Dorovkov, Maxim V. ^{[4
]}

Figdor, Carl G. ^{[2
]}

Ryazanov, Alexey G. ^{[4
]}

Lasonder, Edwin ^{[3
]}

van Leeuwen, Frank N. ^{[1
]}

机构：

[1] Radboud Univ Nijmegen, Med Ctr, Nijmegen Ctr Mol Life Sci, Lab Pediat Oncol, NL-6500 HB Nijmegen, Netherlands

[2] Radboud Univ Nijmegen, Med Ctr, Nijmegen Ctr Mol Life Sci, Dept Tumor Immunol, NL-6500 HB Nijmegen, Netherlands

[3] Radboud Univ Nijmegen, Med Ctr, Nijmegen Ctr Mol Life Sci, Ctr Mol & Biomol Informat, NL-6500 HB Nijmegen, Netherlands

[4] Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Dept Pharmacol, Piscataway, NJ 08854 USA

来源：

FEBS LETTERS | 2008年 / 582卷 / 20期

关键词：

alpha-kinase; TRPM6; TRPM7; myosin II; phosphorylation;

D O I：

10.1016/j.febslet.2008.07.043

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：2993 / 2997

页数：5

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