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| Title: | The alpha-kinases TRPM6 and TRPM7, but not eEF-2 kinase, phosphorylate the assembly domain of myosin IIA, IIB and IIC. |
| Author(s): | Clark, K.
Middelbeek, J.
Dorovkov, M.V.
Figdor, C.G. (067631614)
Ryazanov, A.G.
Lasonder, E. (142800759)
Leeuwen, F.N. van (314437290) |
| Publication year: | 2008 |
| Document type: | Article / Letter to editor |
| Journal: | Febs Letters |
| ISSN: | 0014-5793 |
| Volume: | vol. 582 |
| Issue: | iss. 20 |
| Start page: | p. 2993 |
| End page: | p. 2997 |
| 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. |
| Subject: | NCMLS 1: Immunity, infection and tissue repair
NCMLS 2: Metabolism, transport and motion
UMCN 1.4: Immunotherapy, gene therapy and transplantation
UMCN 5.3: Cellular energy metabolism |
| Organization: | UMCN Extern
Paediatrics
CMBI
Tumorimmunology |
| Organization (former): | Bioinformatics (umcn)
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| Appears in Collections: | Academic bibliography
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Please use this identifier to cite or link to this item:
http://hdl.handle.net/2066/70817
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