Biochemistry (Moscow)

, Volume 73, Issue 3, pp 278–282 | Cite as

Membrane localization of the MAK-V protein kinase

  • S. V. Kalinichenko
  • E. V. Korobko
  • I. V. KorobkoEmail author


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.

Key words

protein kinase MAK-V membrane localization ubiquitin-associated domain 





postnuclear supernatant


ubiquitin-associated domain


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Copyright information

© Pleiades Publishing, Ltd. 2008

Authors and Affiliations

  • S. V. Kalinichenko
    • 1
  • E. V. Korobko
    • 1
    • 2
  • I. V. Korobko
    • 1
    • 2
    Email author
  1. 1.Institute of Gene BiologyRussian Academy of SciencesMoscowRussia
  2. 2.University of Oslo, Centre for Medical Studies in RussiaMoscowRussia

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