Endogenous dephosphorylation of synaptosomal calmodulin-dependent protein kinase type II |
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| Authors: | H LeVine N Sahyoun P Cuatrecasas |
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| Affiliation: | 1. College of Food Science and Engineering, Jilin University, Changchun, 130062, China;2. Institute of Agricultural Biotechnology, Jilin Academy of Agricultural Sciences, Changchun, 130033, China;1. School of Mechanical and Automotive Engineering, College of Engineering and Technology, Dilla University, Dilla 419, Ethiopia;2. School of Mechanical and Industrial Engineering, Ethiopian Institute of Technology-Mekelle (EiT-M), Mekelle University, Tigray, Ethiopia;3. Department of Manufacturing Engineering, School of Mechanical Engineering, Vellore Institute of Technology (VIT), Vellore 632014, Tamil Nadu, India;1. Department of Drug Sciences, Medicinal Chemistry Section, University of Catania, Viale A. Doria, 6, 95100, Catania, Italy;2. Department of Drug Sciences, Pharmacology Section, University of Catania, Viale A. Doria, 6, 95100, Catania, Italy;1. Institute of Electronics, Bulgarian Academy of Sciences, 72, Tsarigradsko Chaussee Blvd., 1784 Sofia, Bulgaria;2. Institute of General Physics, Vienna University of Technology, Wiedner Hauptstr. 8-10/134, A-1040 Wien, Austria;3. Spectra-Physics Vienna, Fernkorngasse 10, 1100 Wien, Austria;4. Institute for Electronic Structure and Lasers-FORTH, P.O. Box 1385, Vassilika Vouton, 711 10 Heraklion, Crete, Greece;5. Faculty of Materials Science and Engineering, Warsaw University of Technology, 141 Woloska Str., 02-507 Warsaw, Poland, Poland |
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| Abstract: | Calmodulin-dependent protein kinase Type II autophosphorylation in synaptosomes is localized to the cytoskeleton (synaptic junction), while a potent dephosphorylating activity is present in the lipid bilayer. The dephosphorylating activity is operative in intact synaptosomes and in a reconstitution system comprised of the cytoskeletal and Triton X-100 - soluble fractions. Dephosphorylation is inhibited by EDTA and pyrophosphate, but not by EGTA or NaF. The present characterization of endogenous synaptosomal dephosphorylating activity completes the regulatory cycle operating on this enzyme in which phosphorylation of calmodulin-dependent protein kinase type II inhibits its response to Ca+2 and calmodulin. |
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