The MAK-V protein kinase regulates endocytosis in mouse
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O R I GI N A L P A P E R
I. V. Korobko á E. V. Korobko á S. L. Kiselev
The MAK-V protein kinase regulates endocytosis in mouse
Received: 3 April 2000 / Accepted: 27 April 2000 / Published online: 16 September 2000 Ó Springer-Verlag 2000
Abstract We report the cloning of a mouse cDNA encoding the MAK-V protein kinase, with a putative speci®city for serine/threonine residues. The mak-v gene is transcribed in adult brain and in the mouse embryo from at least 7.5 dpc. Using the yeast two-hybrid system, we showed that MAK-V interacts with Rabaptin-5, a protein which plays an important role in endocytosis. Functional studies of the MAK-V protein suggest that it regulates endocytosis. We also constructed a human mak-v cDNA and localized the human mak-v gene at 21q22.11. Its chromosomal location suggests that mak-v could be involved in disorders of the nervous system, development or in malignancies. Key words Protein kinase á Endocytosis á Rabaptin-5 á Human chromosome 21q22.11
Introduction Protein phosphorylation is one of the key trigger mechanisms that regulates cell activity. Phosphorylation allows rapid switching of protein state and activity, and requires small amounts of regulator molecules, as signal ampli®cation occurs because each protein kinase molecule is capable of phosphorylating more than one substrate molecule. One of the cellular processes in which protein phosphorylation plays an important role is endocytosis, which is coupled to, and balanced by, exocytosis and membrane vesicle recycling (Beauchamp and Woodman 1994; Ayad et al. 1997; Slepnev et al. 1998).
Communicated by G. P. Georgiev I. V. Korobko (&) á E. V. Korobko á S. L. Kiselev Institute of Gene Biology, Russian Academy of Sciences, 34/5 Vavilov St., Moscow 117334, Russia E-mail: [email protected] Tel.: +7-095-1359970; Fax: +7-095-1354105 The ®rst two authors contributed equally to this work
The precise regulation of, and accurate switching between, endocytosis and exocytosis is required under certain circumstances, for example, during neurotransmitter release and recycling, and protein phosphorylation is one way to achieve these goals (Robinson et al. 1994; Fykse 1998). Although much progress has been made in understanding the regulation of the endocytic machinery during the past few years, the overall mechanism of regulation of endocytosis, exocytosis and membrane recycling still remains unknown, and the role of protein kinases in these processes remains to be established. We previously reported the isolation of a cDNA fragment that presumably encodes a novel protein, MAK-V, with a catalytic domain typical for protein kinases (Korobko et al. 1997). Here we report the cloning of a mouse mak-v cDNA and the sequence of its human homologue. Our functional data sugest that MAK-V is involved in regulating the rate of endocytosis in the cell ¯uid-phase. In addition, we localized the human mak-v gene, and its chromosomal location suggests a number of human disorders in which mak-v may be involved.
Materials and methods Plasmids For expressi
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