Effect of mutations imitating the phosphorylation by TRPM7 kinase on the function of the N-terminal domain of tropomodulin

M. V. Dorovkov; S. N. Beznosov; S. Shah; L. Kotlyanskaya; A. S. Kostyukova

doi:10.1134/S0006350908060055

Effect of mutations imitating the phosphorylation by TRPM7 kinase on the function of the N-terminal domain of tropomodulin

M. V. Dorovkov, S. N. Beznosov, S. Shah, L. Kotlyanskaya, A. S. Kostyukova

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

6 Scopus citations

Abstract

It has been shown that tropomodulin 1 is phosphorylated at serine and threonine residues by TRPM7 kinase. The phosphorylation sites for TRPM7 in the N-terminal functional domain of tropomodulin 1 have been identified, which include tropomyosin-binding and actin-capping regions. It has been found that the phosphorylation-mimicking mutation T54E resulted in the loss of capping ability of the N-terminal tropomodulin domain; however, its tropomyosin-binding ability did not change. We further hypothesize that the phosphorylation of tropomodulin by TRPM7 kinase may play a role in the regulation of the dynamics of actin filaments.

Original language	English (US)
Pages (from-to)	500-504
Number of pages	5
Journal	Biophysics
Volume	53
Issue number	6
DOIs	https://doi.org/10.1134/S0006350908060055
State	Published - Dec 2008
Externally published	Yes

Funding

ACKNOWLEDGMENTS The work was financially supported by American Heart Association, UMDNJ and students foundation Aresty.

Keywords

Actin filaments
Kinase
Phosphorylation
TRPM7
Tropomodulin

ASJC Scopus subject areas

Biophysics

Access to Document

10.1134/S0006350908060055

Cite this

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title = "Effect of mutations imitating the phosphorylation by TRPM7 kinase on the function of the N-terminal domain of tropomodulin",

abstract = "It has been shown that tropomodulin 1 is phosphorylated at serine and threonine residues by TRPM7 kinase. The phosphorylation sites for TRPM7 in the N-terminal functional domain of tropomodulin 1 have been identified, which include tropomyosin-binding and actin-capping regions. It has been found that the phosphorylation-mimicking mutation T54E resulted in the loss of capping ability of the N-terminal tropomodulin domain; however, its tropomyosin-binding ability did not change. We further hypothesize that the phosphorylation of tropomodulin by TRPM7 kinase may play a role in the regulation of the dynamics of actin filaments.",

keywords = "Actin filaments, Kinase, Phosphorylation, TRPM7, Tropomodulin",

author = "Dorovkov, {M. V.} and Beznosov, {S. N.} and S. Shah and L. Kotlyanskaya and Kostyukova, {A. S.}",

note = "Funding Information: ACKNOWLEDGMENTS The work was financially supported by American Heart Association, UMDNJ and students foundation Aresty.",

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doi = "10.1134/S0006350908060055",

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T1 - Effect of mutations imitating the phosphorylation by TRPM7 kinase on the function of the N-terminal domain of tropomodulin

AU - Dorovkov, M. V.

AU - Beznosov, S. N.

AU - Shah, S.

AU - Kotlyanskaya, L.

AU - Kostyukova, A. S.

N1 - Funding Information: ACKNOWLEDGMENTS The work was financially supported by American Heart Association, UMDNJ and students foundation Aresty.

PY - 2008/12

Y1 - 2008/12

N2 - It has been shown that tropomodulin 1 is phosphorylated at serine and threonine residues by TRPM7 kinase. The phosphorylation sites for TRPM7 in the N-terminal functional domain of tropomodulin 1 have been identified, which include tropomyosin-binding and actin-capping regions. It has been found that the phosphorylation-mimicking mutation T54E resulted in the loss of capping ability of the N-terminal tropomodulin domain; however, its tropomyosin-binding ability did not change. We further hypothesize that the phosphorylation of tropomodulin by TRPM7 kinase may play a role in the regulation of the dynamics of actin filaments.

AB - It has been shown that tropomodulin 1 is phosphorylated at serine and threonine residues by TRPM7 kinase. The phosphorylation sites for TRPM7 in the N-terminal functional domain of tropomodulin 1 have been identified, which include tropomyosin-binding and actin-capping regions. It has been found that the phosphorylation-mimicking mutation T54E resulted in the loss of capping ability of the N-terminal tropomodulin domain; however, its tropomyosin-binding ability did not change. We further hypothesize that the phosphorylation of tropomodulin by TRPM7 kinase may play a role in the regulation of the dynamics of actin filaments.

KW - Actin filaments

KW - Kinase

KW - Phosphorylation

KW - TRPM7

KW - Tropomodulin

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Effect of mutations imitating the phosphorylation by TRPM7 kinase on the function of the N-terminal domain of tropomodulin

Abstract

Funding

Keywords

ASJC Scopus subject areas

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