ArticleThe Biochemical journal1990
Kinase activity associated with caldesmon is Ca2+/calmodulin-dependent kinase II.
Article in The Biochemical journal, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 31 citations in OpenAlex.
- Activation of MAP kinases and phosphorylation of caldesmon in canine colonic smooth muscle.The Journal of physiology · 1996Article
- The effects of caldesmon extraction on mechanical properties of skinned smooth muscle fibre preparations.Pflugers Archiv : European journal of physiology · 1996Article
- Characterization of Ca2+/calmodulin-dependent protein kinase II from smooth muscle.The Biochemical journal · 1995Article
- Phosphorylation of caldesmon by smooth-muscle casein kinase II.Journal of muscle research and cell motility · 1994Article
- Calmodulin and the regulation of smooth muscle contraction.Molecular and cellular biochemistry · 1994Review
- Reversal of caldesmon binding to myosin with calcium-calmodulin or by phosphorylating caldesmon.The Journal of biological chemistry · 1993Article
- Smooth-muscle caldesmon phosphatase is SMP-I, a type 2A protein phosphatase.The Biochemical journal · 1993Article
- Phosphorylation by casein kinase II affects the interaction of caldesmon with smooth muscle myosin and tropomyosin.The Biochemical journal · 1993Article
- A comparison of the effects of calponin on smooth and skeletal muscle actomyosin systems in the presence and absence of caldesmon.The Biochemical journal · 1992Article
- Phosphorylation of the C-terminal domain of the Na+/H+ exchanger by Ca2+/calmodulin-dependent protein kinase II.The Biochemical journal · 1992Article
- Functional interrelationship between calponin and caldesmon.The Biochemical journal · 1991Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The relationship of the kinase which co-purifies with caldesmon to Ca2+/calmodulin-dependent protein kinase II (CaM-kinase II) was investigated by studying the phosphorylation of bovine brain synapsin I, as well-characterized substrate of CaM-kinase II. Synapsin I is a very good substrate (Km = 90 nM) of the co-purifying kinase, which phosphorylates two sites in synapsin I, both of which are distinct from the single site phosphorylated by cyclic-AMP-dependent protein kinase. Phosphorylation of synapsin I is Ca2(+)- and calmodulin-dependent: half-maximal activation occurs at 0.13 microM-Ca2+ and maximal activity at 0.4 microM-Ca2+. Phosphorylation of the co-purifying kinase slightly enhances the rate, but does not alter the stoichiometry, of subsequent synapsin I phosphorylation; it does, however, circumvent the requirement for Ca2+ and calmodulin. The properties of this kinase therefore closely resemble those of CaM-kinase II, and we conclude that it is probably a smooth-muscle isoenzyme of CaM-kinase II.
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