Structure–function of the multifunctional Ca2+/calmodulin-dependent protein kinase II
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چکیده
منابع مشابه
Structure-function of the multifunctional Ca2+/calmodulin-dependent protein kinase II.
Ca2+/calmodulin (CaM)-dependent protein kinase (CaMKII) is a ubiquitous mediator of Ca2+-linked signalling that phosphorylates a wide range of substrates to co-ordinate and regulate Ca2+-mediated alterations in cellular function. The transmission of information by the kinase from extracellular stimuli and the intracellular Ca2+ rise is not passive. Rather, its multimeric structure and autoregul...
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Regulation of Ca(2+)/calmodulin-dependent protein kinase II is likely based on an auto-inhibitory mechanism in which a segment of the kinase occupies the catalytic site in the absence of calmodulin. We analyze potential auto-inhibitory associations by employing charge reversal and hydrophobic-to-charged residue mutagenesis. We identify interacting amino acid pairs by using double mutants to tes...
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A cyclic nucleotide- and Ca2+-independent protein kinase has been identified and purified from pig liver to apparent homogeneity. This independent protein kinase is basically inactive but can be activated by a 4-min incubation with 0.25 mM ATP and 2 mM Mg2+. This ATP X Mg-mediated activation appears to involve an intramolecular autophosphorylation as it is independent of kinase concentration. P...
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We have investigated the effect of theophylline on the kinetics of the catalytic subunit of protein kinase and related factors in lung tissue. The results show that the point of highest concentration of the C subunit of protein kinase which is active in casein phosphorylation is at 3h of incubation time, but in the presence of 100 Ilg/ InL and 10µg/mL theophylline, this is shifted to I.S an...
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A Ca2+/calmodulin (CaM)-dependent multifunctional protein kinase has been isolated from Aspergillus nidulans and purified to homogeneity. Unlike any CaM-dependent multifunctional protein kinase described previously, the native enzyme from Aspergillus behaves as a monomer. The calculated molecular weight is 41,200. NaDodSO4/PAGE reveals a single protein band with an apparent Mr of 51,000. Two-di...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 2002
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj20020228