-1 - Isoform-specific Phosphorylation of Mglur5 by Pkc Blocks Ca 2+ Oscillation and Oscillatory Translocation of Ca 2+ -dependent Pkc
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چکیده
Running title: PKC subtype-specific control of Ca 2+ oscillation receptor Total number of characters: 33,831-2-SUMMARY Prolonged activation of a metabotropic glutamate receptor, mGluR5a, causes synchronized oscillations in intracellular calcium, inositol 1,4,5-trisphosphate (IP 3) production, and protein kinase C (PKC) activation. Additionally, mGluR5 stimulation elicited cyclical translocations of MARCKS (myristoylated alanine rich C-kinase substrate) which were opposite to that of JPKC (i.e. from plasma membrane to cytosol) and dependent on PKC activity, indicating that MARCKS is repetitively phosphorylated by oscillating JPKC on the plasma membrane. Mutation of mGluR5 Thr840 to aspartate abolished the oscillation of JPKC but the mutation to alanine (T840A) did not.
منابع مشابه
Isoform-specific phosphorylation of metabotropic glutamate receptor 5 by protein kinase C (PKC) blocks Ca2+ oscillation and oscillatory translocation of Ca2+-dependent PKC.
Prolonged activation of metabotropic glutamate receptor 5a (mGluR5a) causes synchronized oscillations in intracellular calcium, inositol 1,4,5-trisphosphate production, and protein kinase C (PKC) activation. Additionally, mGluR5 stimulation elicited cyclical translocations of myristoylated alanine-rich protein kinase C substrate, which were opposite to that of gammaPKC (i.e. from plasma membran...
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