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6844222696
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note
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286 in the autoinhibitory domain of the α isoform of CaM kinase II and at a comparable site in the other isoforms (5).
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16
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0028306195
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0030058273
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Dosemeci, A.1
Albers, R.W.2
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0028219944
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We reasoned that positioning the HA tag in the association domain, at a site where an insert is normally found in some alternatively spliced δ isoforms of the enzyme [P. Mayer, M. Mohlig, H. Schatz, A. Pfeiffer, Biochem. J. 298, 757 (1994)], should provide an exposed tag that would not interfere with assembly of the oligomer or with its catalytic and regulatory functions. Size fractionation chromatography revealed that the HA tag did not affect the oligomerization of the enzyme. Site-directed mutagenesis (with single-stranded M13-α-CaM kinase II cDNA and antisense oligonucleotide 5′-CCCTGGCCTGGTC-CTTCACAGCTGAGCTCCAGGTCCGGCGTAGTC- GGGGACGTCGTAAGGATAAGGAGCTCCATGGG-GCAGGACGGAGGG-3′) was used to insert the HA tag (8) at the COOH-terminus of α-CaM kinase II as described (27). For β-CaM kinase II cDNA (in the SRα expression vector), we used a Transformer site-directed mutagenesis kit (Clontech, Palo Alto, CA) to insert a sense oligonucleotide (5′-CTCCAGT-GGCCCCACTGCAGGGAGCTCCTTATCCGTACG- AGTCCCCGACTACGCCGGACCTGGAGCTCAG-CTGTGGAGCTGCGCCTGGTTTC-3′) encoding the HA tag.
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Mayer, P.1
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Pfeiffer, A.4
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0024693410
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Hanson, P.I.1
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21
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0028973159
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22
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6844219603
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note
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3 (pH 9.6)] at 4°C overnight. Plates or tubing were washed with Pipes saline [50 mM Pipes (pH 7.0), 150 mM NaCl] and then incubated with 3% (w/v) bovine serum albumin (BSA) (ELISA grade, Sigma) in Pipes saline for 1 hour at room temperature.
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23
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6844242527
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COS-7 cell extracts were diluted 1:40 with Pipes saline containing 0.1% BSA, 10% (v/v) glycerol, 1 mM EGTA, 1 mM phenylmethylsulfonyl fluoride, 1 mM dithiothreitol, leupeptin (10 μg/ml), and pepstatin (10 μg/ml) (Sigma) and then incubated in wells or tubing for 2 to 3 hours at 4°C. This procedure allowed approximately 10 to 15% of the kinase present in the extract to bind to the plastic, saturating the coated antibody. The plastic was washed three times with Pipes saline containing 0.1% BSA and 0.1% Tween-20 and once with the same solution without Tween-20 and was then maintained on ice in Pipes saline containing 0.1% BSA until experimental treatment.
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2+-stimulated activity. Incubation of autophosphorylated α-CaM kinase II for up to 2 min did not result in a decrease in autonomous activity, suggesting that little or no phosphatase activity was present together with the immobilized enzyme.
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6844226382
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note
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The flow rate was 5 ml/s, assuring virtually complete (>95%) exchange of solutions inside a tubing (internal diameter, 1.58 mm) 2 cm in length with a 20-ms valve opening or, for most experiments, inside a tubing 4 cm in length with a 50-ms open time (>200 μl of flow through a 15-μl dead volume inside the manifold plus a volume of 80 μl inside the tubing).
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6844246439
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After 100 pulses (50 ms each, 1 Hz) of perfusion solution (30°C), kinase activity in the tubing was 94 ± 5% (n = 6) of that in untreated tubing.
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note
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286-phosphorylated subunit can phosphorylate a neighbor without having to bind calmodulin (7, 8).
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30
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6844238231
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note
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2+ and calmodulin but not ATP, generated no autonomy, and the subsequent response to 1-Hz stimulation did not differ from that obtained without a control pulse (Fig. 3B).
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We confirmed co-assembly of both CaM kinase II isoforms by immunoprecipitation with an antibody to β-CaM kinase II (CB-β-1) [C. Baitinger, J. Alderton, M. Poenie, H. Schulman, R. A. Steinhardt, J. Cell Biol. 111, 1763 (1990)] from a lysate of COS-7 cells transfected with equal amounts of cDNAs encoding HA-tagged α-and β-CaM kinase. Precipitated proteins were separated by SDS-polyacrylamide gel electrophoresis, transferred to a nitrocellulose membrane, and subjected to calmodulin overlay blot analysis (8). Immunoprecipitated α-and β-CaM kinase II heteromers contained approximately equal amounts of each subunit.
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M. MacNicol, A. Bennett Jefferson, H. Schulman, J. Biol. Chem. 265, 18055 (1990); K. Fukunaga, L. Stoppini, E. Miyamoto, D. Muller, ibid. 268, 7863 (1993); A. Barria, D. Muller, V. Derkach, L. C. Griffith, T. R. Soderling, Science 276, 2042 (1997).
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0027471455
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M. MacNicol, A. Bennett Jefferson, H. Schulman, J. Biol. Chem. 265, 18055 (1990); K. Fukunaga, L. Stoppini, E. Miyamoto, D. Muller, ibid. 268, 7863 (1993); A. Barria, D. Muller, V. Derkach, L. C. Griffith, T. R. Soderling, Science 276, 2042 (1997).
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M. MacNicol, A. Bennett Jefferson, H. Schulman, J. Biol. Chem. 265, 18055 (1990); K. Fukunaga, L. Stoppini, E. Miyamoto, D. Muller, ibid. 268, 7863 (1993); A. Barria, D. Muller, V. Derkach, L. C. Griffith, T. R. Soderling, Science 276, 2042 (1997).
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46
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6844228519
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note
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This exponential function is used to illustrate the relation between frequency of stimulation and CaM kinase II autonomy without any implied model. Data were fitted with PSI-PLOT software; the correlations for the fits in Fig. 4 were all ≥0.95, with SSD values of <0.35. The significance of differences between curves was determined with an F test comparing the variance of the pooled data set with the sum of the variance of the individual data sets.
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47
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6844221654
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note
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We thank D. Profitt and R. Schneeveis for building the pulse-flow device; S. Sather for help with site-directed mutagenesis and early studies on immobilized kinase; A. Braun, P. Hanson, T. Meyer, A. Naini, and R. Y. Tsien for helpful discussions; and J. Ferrell and L. Stryer for their comments on the manuscript. Supported by NIH grants GM40600 and GM30179 and by a Human Frontier Science Program Organization fellowship to P.D.K.
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