The alpha-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 alpha-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

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

82 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 alpha-kinases.

Original language	English
Pages (from-to)	2993-7
Number of pages	5
Journal	FEBS letters
Volume	582
Issue number	20
DOIs	https://doi.org/10.1016/j.febslet.2008.07.043
Publication status	Published - 3 Sept 2008
Externally published	Yes

Keywords

Amino Acid Sequence
Cell Line
Elongation Factor 2 Kinase/genetics
Humans
Molecular Sequence Data
Myosin Heavy Chains/metabolism
Myosin Type II/metabolism
Nonmuscle Myosin Type IIA/metabolism
Nonmuscle Myosin Type IIB/metabolism
Phosphorylation
Protein Serine-Threonine Kinases
Protein Structure, Tertiary
TRPM Cation Channels/genetics

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10.1016/j.febslet.2008.07.043

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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",

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.",

keywords = "Amino Acid Sequence, Cell Line, Elongation Factor 2 Kinase/genetics, Humans, Molecular Sequence Data, Myosin Heavy Chains/metabolism, Myosin Type II/metabolism, Nonmuscle Myosin Type IIA/metabolism, Nonmuscle Myosin Type IIB/metabolism, Phosphorylation, Protein Serine-Threonine Kinases, Protein Structure, Tertiary, TRPM Cation Channels/genetics",

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--7",

journal = "FEBS letters",

issn = "0014-5793",

publisher = "John Wiley and Sons Inc.",

number = "20",

}

TY - JOUR

T1 - The alpha-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 alpha-kinases.

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 alpha-kinases.

KW - Amino Acid Sequence

KW - Cell Line

KW - Elongation Factor 2 Kinase/genetics

KW - Humans

KW - Molecular Sequence Data

KW - Myosin Heavy Chains/metabolism

KW - Myosin Type II/metabolism

KW - Nonmuscle Myosin Type IIA/metabolism

KW - Nonmuscle Myosin Type IIB/metabolism

KW - Phosphorylation

KW - Protein Serine-Threonine Kinases

KW - Protein Structure, Tertiary

KW - TRPM Cation Channels/genetics

UR - https://www.scopus.com/pages/publications/49649103081

U2 - 10.1016/j.febslet.2008.07.043

DO - 10.1016/j.febslet.2008.07.043

M3 - Article

C2 - 18675813

SN - 0014-5793

VL - 582

SP - 2993

EP - 2997

JO - FEBS letters

JF - FEBS letters

IS - 20

ER -

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

Abstract

Keywords

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