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Membrane Localization of the MAK-V Protein Kinase

S. V. Kalinichenko1, E. V. Korobko1,2, and I. V. Korobko1,2*

1Institute of Gene Biology, Russian Academy of Sciences, ul. Vavilova 34/5, 119334 Moscow, Russia; fax: (499) 135-4105; E-mail: igorvk@igb.ac.ru

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

* To whom correspondence should be addressed.

Received September 4, 2007
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

DOI: 10.1134/S000629790803061