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

Kristopher Clark; Jeroen Middelbeek; Maxim V. Dorovkov; Carl G. Figdor; Alexey G. Ryazanov; Edwin Lasonder; Frank N. van Leeuwen

doi:10.1016/j.febslet.2008.07.043

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

Kristopher Clark, Jeroen Middelbeek, Maxim V. Dorovkov, Carl G. Figdor, Alexey G. Ryazanov, Edwin Lasonder, Frank N. van Leeuwen^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

68 Citations (Scopus)

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 α-kinases. Structured summary: MINT-6700314:GNA1 (uniprotkb:Q96EK6) and GNA1 (uniprotkb:Q96EK6) bind (MI:0407) by X-ray crystallography (MI:0114).

Original language	English
Pages (from-to)	2993-2997
Number of pages	5
Journal	FEBS Letters
Volume	582
Issue number	20
Early online date	1 Aug 2008
DOIs	https://doi.org/10.1016/j.febslet.2008.07.043
Publication status	Published - 3 Sep 2008
Externally published	Yes

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10.1016/j.febslet.2008.07.043

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

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 α-kinases. Structured summary: MINT-6700314:GNA1 (uniprotkb:Q96EK6) and GNA1 (uniprotkb:Q96EK6) bind (MI:0407) by X-ray crystallography (MI:0114).",

keywords = "α-Kinase, Myosin II, Phosphorylation, TRPM6, TRPM7",

author = "Kristopher Clark and Jeroen Middelbeek and Dorovkov, {Maxim V.} and Figdor, {Carl G.} and Ryazanov, {Alexey G.} and Edwin Lasonder and {van Leeuwen}, {Frank N.}",

note = "Funding information: We thank Niels Peterse for technical assistance. This work was supported by Grants from the Dutch Cancer Society to FNvL.",

year = "2008",

month = sep,

day = "3",

doi = "10.1016/j.febslet.2008.07.043",

language = "English",

volume = "582",

pages = "2993--2997",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Elsevier",

number = "20",

}

TY - JOUR

T1 - The α-kinases TRPM6 and TRPM7, but not eEF-2 kinase, phosphorylate the assembly domain of myosin IIA, IIB and IIC

AU - Clark, Kristopher

AU - Middelbeek, Jeroen

AU - Dorovkov, Maxim V.

AU - Figdor, Carl G.

AU - Ryazanov, Alexey G.

AU - Lasonder, Edwin

AU - van Leeuwen, Frank N.

N1 - Funding information: We thank Niels Peterse for technical assistance. This work was supported by Grants from the Dutch Cancer Society to FNvL.

PY - 2008/9/3

Y1 - 2008/9/3

N2 - 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 α-kinases. Structured summary: MINT-6700314:GNA1 (uniprotkb:Q96EK6) and GNA1 (uniprotkb:Q96EK6) bind (MI:0407) by X-ray crystallography (MI:0114).

AB - 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 α-kinases. Structured summary: MINT-6700314:GNA1 (uniprotkb:Q96EK6) and GNA1 (uniprotkb:Q96EK6) bind (MI:0407) by X-ray crystallography (MI:0114).

KW - α-Kinase

KW - Myosin II

KW - Phosphorylation

KW - TRPM6

KW - TRPM7

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U2 - 10.1016/j.febslet.2008.07.043

DO - 10.1016/j.febslet.2008.07.043

M3 - Article

C2 - 18675813

AN - SCOPUS:49649103081

VL - 582

SP - 2993

EP - 2997

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 20

ER -

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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