Please use this identifier to cite or link to this item:
https://doi.org/10.1083/jcb.200409157
DC Field | Value | |
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dc.title | Reversible intracellular translocation of KRas but not HRas in hippocampal neurons regulated by Ca2+/calmodulin | |
dc.contributor.author | Fivaz, M | |
dc.contributor.author | Meyer, T | |
dc.date.accessioned | 2020-10-27T09:47:15Z | |
dc.date.available | 2020-10-27T09:47:15Z | |
dc.date.issued | 2005 | |
dc.identifier.citation | Fivaz, M, Meyer, T (2005). Reversible intracellular translocation of KRas but not HRas in hippocampal neurons regulated by Ca2+/calmodulin. Journal of Cell Biology 170 (3) : 429-441. ScholarBank@NUS Repository. https://doi.org/10.1083/jcb.200409157 | |
dc.identifier.issn | 00219525 | |
dc.identifier.uri | https://scholarbank.nus.edu.sg/handle/10635/181087 | |
dc.description.abstract | The Ras/MAPK pathway regulates synaptic plasticity and cell survival in neurons of the central nervous system. Here, we show that KRas, but not HRas, acutely translocates from the plasma membrane (PM) to the Golgi complex and early/recycling endosomes in response to neuronal activity. Translocation is reversible and mediated by the polybasic-prenyl membrane targeting motif of KRas. We provide evidence that KRas translocation occurs through sequestration of the polybasic-prenyl motif by Ca2+/calmodulin (Ca 2+/CaM) and subsequent release of KRas from the PM, in a process reminiscent of GDP dissociation inhibitor-mediated membrane recycling of Rab and Rho GTPases. KRas translocation was accompanied by partial intracellular redistribution of its activity. We conclude that the polybasic-prenyl motif acts as a Ca2+/CaM-regulated molecular switch that controls PM concentration of KRas and redistributes its activity to internal sites. Our data thus define a novel signaling mechanism that differentially regulates KRas and HRas localization and activity in neurons. © The Rockefeller University Press. | |
dc.rights | Attribution 4.0 International | |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | |
dc.source | Unpaywall 20201031 | |
dc.subject | calcium | |
dc.subject | calmodulin | |
dc.subject | guanine nucleotide dissociation inhibitor | |
dc.subject | Rab protein | |
dc.subject | Ras protein | |
dc.subject | Rho guanine nucleotide binding protein | |
dc.subject | animal cell | |
dc.subject | article | |
dc.subject | cell membrane | |
dc.subject | controlled study | |
dc.subject | endosome | |
dc.subject | Golgi complex | |
dc.subject | hippocampus | |
dc.subject | nerve cell | |
dc.subject | nonhuman | |
dc.subject | priority journal | |
dc.subject | protein localization | |
dc.subject | rat | |
dc.subject | Animals | |
dc.subject | Calcium | |
dc.subject | Calmodulin | |
dc.subject | Cell Membrane | |
dc.subject | Cells, Cultured | |
dc.subject | Endosomes | |
dc.subject | Glutamic Acid | |
dc.subject | Golgi Apparatus | |
dc.subject | GTP Phosphohydrolases | |
dc.subject | Hippocampus | |
dc.subject | Humans | |
dc.subject | Mutation | |
dc.subject | Neurons | |
dc.subject | Protein Isoforms | |
dc.subject | Protein Transport | |
dc.subject | ras Proteins | |
dc.subject | Rats | |
dc.subject | Signal Transduction | |
dc.type | Article | |
dc.contributor.department | DUKE-NUS MEDICAL SCHOOL | |
dc.description.doi | 10.1083/jcb.200409157 | |
dc.description.sourcetitle | Journal of Cell Biology | |
dc.description.volume | 170 | |
dc.description.issue | 3 | |
dc.description.page | 429-441 | |
Appears in Collections: | Elements Staff Publications |
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