| Literature DB >> 18675813 |
Kristopher Clark1, Jeroen Middelbeek, Maxim V Dorovkov, Carl G Figdor, Alexey G Ryazanov, Edwin Lasonder, Frank N van Leeuwen.
Abstract
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.Entities:
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Year: 2008 PMID： 18675813 DOI： 10.1016/j.febslet.2008.07.043
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124