These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Ca(2+)-independent autophosphorylation of postsynaptic density-associated Ca2+/calmodulin-dependent protein kinase.
    Author: Dosemeci A, Choi C.
    Journal: Neurochem Res; 1997 Sep; 22(9):1151-7. PubMed ID: 9251106.
    Abstract:
    A major protein in the postsynaptic density fraction is alpha-CAM kinase II, the alpha-subunit of the Ca2+/calmodulin-dependent protein kinase. Autophosphorylation of the postsynaptic density-associated CaM kinase II is likely to be a crucial event in the induction of activity-dependent synaptic modification. This study focuses on the regulation and consequences of Ca(2+)-independent autophosphorylation of the enzyme. In isolated postsynaptic densities, a sub-stochiometric level of autophosphorylation in the presence of Ca2+ is sufficient to trigger maximal Ca(2+)-independent autophosphorylation of alpha-CaM Kinase II. A major fraction of the sites phosphorylated in the absence of Ca2+ can be dephosphorylated by the endogenous phosphatase activity in the preparation. Ca(2+)-independent autophosphorylation is correlated with a drastic decrease in calmodulin binding to postsynaptic densities. This may represent a physiological mechanism that lower the calmodulin trapping capacity of the organelle, thus increasing the availability of calmodulin to other elements within a spine.
    [Abstract] [Full Text] [Related] [New Search]