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The Journal of Neuroscience, September 1, 2002, 22(17):7331-7339
Reversible Translocation and Activity-Dependent Localization of the Calcium-Myristoyl Switch Protein VILIP-1 to Different Membrane Compartments in Living Hippocampal Neurons
Christina Spilker1, 2, Thomas Dresbach2, and Karl-Heinz Braunewell1 1 Neuroscience Research Center-Institute for Physiology of the Charite, Humboldt University Berlin, Signal Transduction Research Group, D-10117 Berlin, Germany, and 2 Leibniz Institute for Neurobiology, Department of Neurochemistry/Molecular Biology, D-39118 Magdeburg, Germany
Visinin-like protein-1 (VILIP-1) belongs to the family of neuronal calcium sensor (NCS) proteins, a neuronal subfamily of EI-hand calcium-binding proteins that are myristoylated at their N termini. NCS proteins are discussed to play roles in calcium-dependent signal transduction of physiological and pathological processes in the CNS. The calcium-dependent membrane association, the so-called calcium-myristoyl switch, localizes NCS proteins to a distinct cellular signaling compartment and thus may be a critical mechanism for the coordinated regulation of signaling cascades. To study whether the biochemically defined calcium-myristoyl switch of NCS proteins can occur in living neuronal cells, the reversible and stimulus-dependent translocation of green fluorescent protein (GFP)-tagged VILIP-1 to subcellular targets was examined by fluorescence microscopy in transfected cell lines and hippocampal primary neurons. In transiently transfected NG108-15 and COS-7 cells, a translocation of diffusely distributed VILIP-1-GFP but not of myristoylation-deficient VILIP-1-GFP to the plasma membrane and to intracellular targets, such as Golgi membranes, occurred after raising the intracellular calcium concentration with a calcium ionophore. The observed calcium-dependent localization was completely reversed after depletion of intracellular calcium by EGTA. Interestingly, a fast and reversible translocation of VILIP-1-GFP and translocation of endogenous VILIP-1 to specialized membrane structures was also observed after a depolarizing stimulus or activation of glutamate receptors in hippocampal neurons. These results show for the first time the reversibility and stimulus-dependent occurrence of the calcium-myristoyl switch in living neurons, suggesting a physiological role as a signaling mechanism of NCS proteins, enabling them to activate specific targets localized in distinct membrane compartments.
Key words: activity-dependent; calcium-myristoyl switch; hippocampal neurons; GFP; Golgi; membrane compartments; NCS protein; signaling; VILIP-1
Copyright © 2002 Society for Neuroscience 0270-6474/02/22177331-09$05.00/0
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