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Membrane localization of the MAK-V protein kinase

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Abstract

Activities of many proteins including protein kinases are often regulated by their dynamic association with specific intracellular compartments. MAK-V is an AMPK-like protein kinase with poorly characterized functions and mechanisms of action. Similarly to many other protein kinases, association of MAK-V with specific intracellular compartments could be essential for its proper functions. In this work, we studied subcellular distribution of exogenously produced and endogenous MAK-V proteins in mammalian cells using biochemical cell fractioning aiming to supplement data on MAK-V intracellular localization studied by immunocytochemical methods. We found that a significant portion of MAK-V protein in mammalian cells is associated with membranes. Moreover, MAK-V expressed in yeast was also targeted to membrane, thus suggesting an evolutionarily conservative mechanism of MAK-V membrane association. Based on the ability of various MAK-V deletion mutants to localize to membrane and comparison of MAK-V amino acid sequences from different species, we suggest a possible mechanism governing MAK-V association with intracellular membranes.

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Abbreviations

PI(4,5)P2 :

phosphatidylinositol-(4,5)-bisphosphate

PNS:

postnuclear supernatant

UBA:

ubiquitin-associated domain

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Authors and Affiliations

  1. Institute of Gene Biology, Russian Academy of Sciences, ul. Vavilova 34/5, 119334, Moscow, Russia

    S. V. Kalinichenko, E. V. Korobko & I. V. Korobko

  2. University of Oslo, Centre for Medical Studies in Russia, ul. Vavilova 34/5, 119334, Moscow, Russia

    E. V. Korobko & I. V. Korobko

Authors
  1. S. V. Kalinichenko
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  2. E. V. Korobko
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  3. I. V. Korobko
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Correspondence to I. V. Korobko.

Additional information

Published in Russian in Biokhimiya, 2008, Vol. 73, No. 3, pp. 342–348.

Originally published in Biochemistry (Moscow) On-Line Papers in Press, as Manuscript BM07-294, November 11, 2007.

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Kalinichenko, S.V., Korobko, E.V. & Korobko, I.V. Membrane localization of the MAK-V protein kinase. Biochemistry Moscow 73, 278–282 (2008). https://doi.org/10.1134/S0006297908030061

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  • DOI: https://doi.org/10.1134/S0006297908030061

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