Abstract
The protein kinase C (PKC) family has been implicated in a large number of cellular responses. In order to better understand the cellular function of these enzymes, the identification of physiologically important substrates has received a peculiar attention during the last decade. The myristoylated alanine-rich C kinase substrate (MARCKS) is a widely distributed in vivo and in vitro substrate that has been often used as a marker of the activation of the kinase. (see Aderem, 1992 and Blackshear, 1993). Its phosphorylation by PKC in the cells leads to its translocation from the plasma membrane to the cytoplasmic compartment. The process is reversible, the dephosphorylation by cellular phosphatases leading to its reassociation with the plasma membrane (Thelen et al., 1991).
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Manenti, S., Sorokine, O., Van Dorsselaer, A., Taniguchi, H. (1994). Marcks, a Major in Vivo Substrate of Protein Kinase C Purification, Interaction with Model Membrane, and Demyristoylation. In: Municio, A.M., Miras-Portugal, M.T. (eds) Cell Signal Transduction, Second Messengers, and Protein Phosphorylation in Health and Disease. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1879-2_7
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DOI: https://doi.org/10.1007/978-1-4615-1879-2_7
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