Journal article
Phosphorylation of the 1,4-dihydropyridine receptor of the voltage dependent Ca2+ channel by an intrinsic protein kinase in isolated triads from rabbit skeletal muscle
The Journal of biological chemistry, Vol.262(17), pp.8333-8339
1987
DOI: 10.1016/S0021-9258(18)47568-0
PMID: 2439499
Abstract
Isolated triads from rabbit skeletal muscle were shown to contain an intrinsic protein kinase which was neither Ca2+/calmodulin-dependent nor cAMP-dependent. The protein substrates phosphorylated by this protein kinase exhibited apparent molecular weights of 300,000, 170,000, 90,000, 80,000, 65,000, 56,000, 52,000, 51,000, 40,000, 25,000, 22,000, and 15,000. Purification of the 1,4-dihydropyridine receptor from phosphorylated triads has demonstrated that the 170,000- and 52,000-Da subunits of the 1,4-dihydropyridine receptor are phosphorylated by this intrinsic protein kinase in isolated triads. Monoclonal antibodies to the 170,000-Da subunit of the dihydropyridine receptor immunoprecipitated the 170,000-Da phosphoprotein from detergent extracts of phosphorylated triads. The mobility of the 170,000-Da phosphoprotein in sodium dodecyl sulfate-polyacrylamide gels was not changed with or without reduction, demonstrating that the 170,000-Da phosphoprotein is not the glycoprotein subunit of the receptor. Our results demonstrate that the 170,000- and 52,000-Da subunits of the dihydropyridine receptor are phosphorylated by an intrinsic protein kinase in isolated triads. In addition, our results also demonstrate that the 175,000-Da glycoprotein subunit of the dihydropyridine receptor is not phosphorylated in isolated triads by the intrinsic protein kinase, cAMP-dependent protein kinase, or endogenous Ca2+/calmodulin-dependent protein kinase.
Details
- Title: Subtitle
- Phosphorylation of the 1,4-dihydropyridine receptor of the voltage dependent Ca2+ channel by an intrinsic protein kinase in isolated triads from rabbit skeletal muscle
- Creators
- Toshiaki Imagawa - Univ. Iowa, dep. physiology biophysics, Iowa City IA 52242, United StatesAlbert T Leung - Univ. Iowa, dep. physiology biophysics, Iowa City IA 52242, United StatesKevin P Campbell - Univ. Iowa, dep. physiology biophysics, Iowa City IA 52242, United States
- Resource Type
- Journal article
- Publication Details
- The Journal of biological chemistry, Vol.262(17), pp.8333-8339
- DOI
- 10.1016/S0021-9258(18)47568-0
- PMID
- 2439499
- NLM abbreviation
- J Biol Chem
- ISSN
- 0021-9258
- eISSN
- 1083-351X
- Publisher
- American Society for Biochemistry and Molecular Biology; Bethesda, MD
- Language
- English
- Date published
- 1987
- Academic Unit
- Neurology; Molecular Physiology and Biophysics; Iowa Neuroscience Institute
- Record Identifier
- 9984068262102771
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