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

  • Molecular Biophysics
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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.

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Abbreviations

PCR:

polymerase chain reaction

SDS:

sodium dodecyl sulfate

PAAG:

polyacrylamid gel

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Authors and Affiliations

  1. Department of Pharmacology, RW JMS, UMDJN, 675 Hoes Lane, Piscataway, NJ, 08854, USA

    M. V. Dorovkov

  2. Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow region, 142290, Russia

    S. N. Beznosov & A. S. Kostyukova

  3. Department of Neuroscience and Cell Biology, RW JMS, UMDJN, 675 Hoes Lane, Piscataway, NJ, 08854, USA

    S. Shah, L. Kotlyanskaya & A. S. Kostyukova

Authors
  1. M. V. Dorovkov
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  2. S. N. Beznosov
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  3. S. Shah
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  4. L. Kotlyanskaya
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  5. A. S. Kostyukova
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Additional information

Original Russian Text © M.V. Dorovkov, S.N. Beznosov, S. Shah, L. Kotlyanskaya, A.S. Kostyukova, 2008, published in Biofizika, 2008, Vol. 53, No. 6, pp. 943–949.

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Dorovkov, M.V., Beznosov, S.N., Shah, S. et al. Effect of mutations imitating the phosphorylation by TRPM7 kinase on the function of the N-terminal domain of tropomodulin. BIOPHYSICS 53, 500–504 (2008). https://doi.org/10.1134/S0006350908060055

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  • DOI: https://doi.org/10.1134/S0006350908060055

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