Linked Life Data

12196554

Source:http://linkedlifedata.com/resource/pubmed/id/12196554

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
2002-8-27
pubmed:abstractText
Visinin-like protein-1 (VILIP-1) belongs to the family of neuronal calcium sensor (NCS) proteins, a neuronal subfamily of EF-hand [corrected] 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.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1529-2401
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
22
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7331-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:12196554-Animals, pubmed-meshheading:12196554-COS Cells, pubmed-meshheading:12196554-Calcium, pubmed-meshheading:12196554-Calcium-Binding Proteins, pubmed-meshheading:12196554-Cell Compartmentation, pubmed-meshheading:12196554-Cell Line, pubmed-meshheading:12196554-Green Fluorescent Proteins, pubmed-meshheading:12196554-Hippocampus, pubmed-meshheading:12196554-Internet, pubmed-meshheading:12196554-Intracellular Fluid, pubmed-meshheading:12196554-Intracellular Membranes, pubmed-meshheading:12196554-Luminescent Proteins, pubmed-meshheading:12196554-Mice, pubmed-meshheading:12196554-Microscopy, Fluorescence, pubmed-meshheading:12196554-Microscopy, Video, pubmed-meshheading:12196554-Myristates, pubmed-meshheading:12196554-Nerve Tissue Proteins, pubmed-meshheading:12196554-Neurocalcin, pubmed-meshheading:12196554-Neurons, pubmed-meshheading:12196554-Protein Transport, pubmed-meshheading:12196554-Rats, pubmed-meshheading:12196554-Receptors, Calcium-Sensing, pubmed-meshheading:12196554-Recombinant Fusion Proteins, pubmed-meshheading:12196554-Signal Transduction, pubmed-meshheading:12196554-Transfection, pubmed-meshheading:12196554-Video Recording
pubmed:year
2002
pubmed:articleTitle
Reversible translocation and activity-dependent localization of the calcium-myristoyl switch protein VILIP-1 to different membrane compartments in living hippocampal neurons.
pubmed:affiliation
Neuroscience Research Center-Institute for Physiology of the Charite, Humboldt University Berlin, Signal Transduction Research Group, D-10117 Berlin, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't