• Login
    About WHOAS
    View Item 
    •   WHOAS Home
    • Marine Biological Laboratory
    • Program in Molecular Physiology
    • View Item
    •   WHOAS Home
    • Marine Biological Laboratory
    • Program in Molecular Physiology
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of WHOASCommunities & CollectionsBy Issue DateAuthorsTitlesKeywordsThis CollectionBy Issue DateAuthorsTitlesKeywords

    My Account

    LoginRegister

    Statistics

    View Usage Statistics

    Inhibition of phosphatase activity facilitates the formation and maintenance of NMDA-induced calcium/calmodulin-dependent protein kinase ii clusters in hippocampal neurons

    Thumbnail
    View/Open
    Author's final draft (76.5Kb)
    Figure 1: CaMKII clusters are phosphorylated (227.5Kb)
    Figure 2: CaMKII clustering is maintained in the presence of phosphatase inhibitors (506.2Kb)
    Date
    2004-10-04
    Author
    Tao-Cheng, Jung-Hwa  Concept link
    Vinade, Lucia  Concept link
    Winters, Christine A.  Concept link
    Reese, Thomas S.  Concept link
    Dosemeci, Ayse  Concept link
    Metadata
    Show full item record
    Citable URI
    https://hdl.handle.net/1912/607
    As published
    https://doi.org/10.1016/j.neuroscience.2004.10.008
    Keyword
     Immunogold electron microscopy; Calyculin A; Okadaic acid; Calcium/calmodulin-dependent protein kinase II; Autophosphorylation 
    Abstract
    The majority of hippocampal neurons in dissociated cultures and in intact brain exhibit clustering of CaMKII into spherical structures with an average diameter of 110 nm when subjected to conditions that mimic ischemia and excitotoxicity (Tao-Cheng et al., 2001). Because clustering of CaMKII would reduce its effective concentration within the neuron, it may represent a cellular strategy to prevent excessive CaMKII-mediated phosphorylation during episodes of Ca2+ overload. Here we employ a relatively mild excitatory stimulus to promote sub-maximal clustering for the purpose of studying the conditions for the formation and disappearance of CaMKII clusters. Treatment with 30 µM NMDA for 2 min produced CaMKII clustering in ~15 percent of dissociated hippocampal neurons in culture, as observed by pre-embedding immunogold electron microscopy. These CaMKII clusters could be labeled with antibodies specific to the phospho form (Thr286) of CaMKII, suggesting that at least some of the CaMKII molecules in clusters are autophosphorylated. To test whether phosphorylation is involved in the formation and maintenance of CaMKII clusters, the phosphatase inhibitors calyculin A (5 nM) or okadaic acid (1 µM) were included in the incubation medium. With inhibitors more neurons exhibited CaMKII clusters in response to 2 min NMDA treatment. Furthermore, 5 min after the removal of NMDA and Ca2+, CaMKII clusters remained and could still be labeled with the phospho-specific antibody. In contrast, in the absence of phosphatase inhibitors, no clusters were detected 5 min after the removal of NMDA and Ca2+ from the medium. These results suggest that phosphatases type 1 and/or 2A regulate the formation and disappearance of CaMKII clusters.
    Description
    Author Posting. © The Authors, 2004. This is the author's version of the work. It is posted here by permission of Elsevier B. V. for personal use, not for redistribution. The definitive version was published in Neuroscience 130 (2005), doi:10.1016/j.neuroscience.2004.10.008.
    Collections
    • Program in Molecular Physiology
    Suggested Citation
    Preprint: Tao-Cheng, Jung-Hwa, Vinade, Lucia, Winters, Christine A., Reese, Thomas S., Dosemeci, Ayse, "Inhibition of phosphatase activity facilitates the formation and maintenance of NMDA-induced calcium/calmodulin-dependent protein kinase ii clusters in hippocampal neurons", 2004-10-04, https://doi.org/10.1016/j.neuroscience.2004.10.008, https://hdl.handle.net/1912/607
     

    Related items

    Showing items related by title, author, creator and subject.

    • Thumbnail

      Persistent accumulation of calcium/calmodulin-dependent protein kinase II in dendritic spines after induction of NMDA receptor-dependent chemical long-term potentiation 

      Otmakhov, Nikolai; Tao-Cheng, Jung-Hwa; Carpenter, Stephen; Asrican, Brent; Dosemeci, Ayse; Reese, Thomas S.; Lisman, John E. (Society for Neuroscience, 2004-10-20)
      Calcium/calmodulin-dependent protein kinase II (CaMKII) is a leading candidate for a synaptic memory molecule because it is persistently activated after long-term potentiation (LTP) induction and because mutations that ...
    • Thumbnail

      Distribution of postsynaptic density (PSD)-95 and Ca2+/calmodulin-dependent protein kinase II at the PSD 

      Petersen, Jennifer D.; Chen, Xiaobing; Vinade, Lucia; Dosemeci, Ayse; Lisman, John E.; Reese, Thomas S. (Society for Neuroscience, 2003-12-03)
      Postsynaptic densities (PSDs) contain proteins that regulate synaptic transmission. We determined the positions of calcium/calmodulin-dependent protein kinase II (CaMKII) and PSD-95 within the three-dimensional structure ...
    • Thumbnail

      Prion protein inhibits fast axonal transport through a mechanism involving casein kinase 2 

      Zamponi, Emiliano; Buratti, Fiamma; Cataldi, Gabriel; Caicedo, Hector Hugo; Song, Yuyu; Jungbauer, Lisa M.; LaDu, Mary J.; Bisbal, Mariano; Lorenzo, Lorenzo; Ma, Jiyan; Helguera, Pablo R.; Morfini, Gerardo A.; Brady, Scott T.; Pigino, Gustavo F. (Public Library of Science, 2017-12-20)
      Prion diseases include a number of progressive neuropathies involving conformational changes in cellular prion protein (PrPc) that may be fatal sporadic, familial or infectious. Pathological evidence indicated that neurons ...
    All Items in WHOAS are protected by original copyright, with all rights reserved, unless otherwise indicated. WHOAS also supports the use of the Creative Commons licenses for original content.
    A service of the MBLWHOI Library | About WHOAS
    Contact Us | Send Feedback | Privacy Policy
    Core Trust Logo