Table S1
ID |
Reaction name |
Kinetic parameters |
References |
||
a1 |
PKC_bind_Ca |
kf = 0.25 sec-1mM-2 |
kb = 1 sec-1 |
Kd = 2 mM |
1 |
a2 |
PKC-Ca_memb |
kf = 1 sec-1 |
kb = 0.1 sec-1 |
Keq = 10 |
1 |
a3 |
PKC_bind_AA |
kf = 0.2 sec-1mM-1 |
kb = 10 sec-1 |
Kd = 50 mM |
2 |
a4 |
PKC-AA_bind_Ca |
kf = 0.25 sec-1mM-2 |
kb = 1 sec-1 |
Kd = 2 mM |
1 |
a5 |
PKC-Ca_bind_AA |
kf = 0.2 sec-1mM-1 |
kb = 10 sec-1 |
Kd = 50 mM |
2 |
b1 |
PKC_phos_Raf |
Km = 11.5 mM |
kcat = 0.0335 sec-1 |
k-1/kcat = 4 |
3, 4 |
b2 |
PP2A_deph_Raf-P |
Km = 15.7 mM |
kcat = 6 sec-1 |
k-1/kcat = 4 |
5 |
b3 |
Raf_act_MEK |
Km = 0.398 mM |
kcat = 0.105 sec-1 |
k-1/kcat = 4 |
6 |
b4 |
Raf_act_MEK-P |
Km = 0.398 mM |
kcat = 0.105 sec-1 |
k-1/kcat = 4 |
6 |
b5 |
PP2A_deph_MEK-PP |
Km = 15.7 mM |
kcat = 6 sec-1 |
k-1/kcat = 4 |
5, 7, 8 |
b6 |
PP2A_deph_MEK-P |
Km = 15.7 mM |
kcat = 6 sec-1 |
k-1/kcat = 4 |
5, 7, 8 |
b7 |
MEK_act_MAPK |
Km = 0.0463 mM |
kcat = 0.15 sec-1 |
k-1/kcat = 4 |
9, 10 |
b8 |
MEK_act_MAPK-P |
Km = 0.0463 mM |
kcat = 0.15 sec-1 |
k-1/kcat = 4 |
9, 10 |
b9 |
MKP_deph_MAPK-PP |
Km = 0.16667 mM |
kcat = 1 sec-1 |
k-1/kcat = 4 |
11, 12 |
b10 |
MKP_deph_MEPK-P |
Km = 0.16667 mM |
kcat = 1 sec-1 |
k-1/kcat = 4 |
11, 12 |
c1 |
MAPK_phos_PLA2 |
Km = 25.6 mM |
kcat = 20 sec-1 |
k-1/kcat = 4 |
13, 14 |
c2 |
PLA2-P_deg |
kf = 0.17 sec-1 |
kb = 0 sec-1 |
|
15 |
c3 |
PLA2_bind_Ca |
kf = 0.01 sec-1 |
kb = 0.1 sec-1 |
Kd = 10 mM |
16 |
c4 |
PLA2-PIP2_bind_Ca |
kf = 0.01 sec-1 |
kb = 0.1 sec-1 |
Kd = 10 mM |
16 |
c5 |
PLA2_bind_PIP2 |
kf = 0.0012 sec-1 |
kb = 0.48 sec-1 |
Kd = 400 mM |
4 |
c6 |
PLA2-Ca_bind_PIP2 |
kf = 0.0012 sec-1 |
kb = 0.48 sec-1 |
Kd = 400 mM |
4 |
c7 |
PLA2-Ca_prd_AA |
Km = 20 mM |
kcat = 54 sec-1 |
k-1/kcat = 4 |
17 |
c8 |
PLA2-PIP2_prd_AA |
Km = 20 mM |
kcat = 11.04 sec-1 |
k-1/kcat = 4 |
17 |
c9 |
PLA2-PIP2-Ca_prd_AA |
Km = 20 mM |
kcat = 36 sec-1 |
k-1/kcat = 4 |
17 |
c10 |
PLA2-P_prd_AA |
Km = 20 mM |
kcat = 120 sec-1 |
k-1/kcat = 4 |
17 |
c11 |
AA_deg |
kf = 0.4 sec-1 |
kb = 0 sec-1 |
|
15 |
d1 |
PKC_phos_AMPAR |
Km = 3.5 mM |
kcat = 0.05 sec-1 |
k-1/kcat = 4 |
4 |
d2 |
PP2A_deph_AMPAR-P |
Km = 15.7 mM |
kcat = 6 sec-1 |
k-1/kcat = 4 |
5 |
kf and kb are defined by the formula S8. k1, k-1, and kcat are defined by the formula S9. Kd: dissociation constant (Kd = kb/kf) Keq: equilibrium constant (Keq = kb/kf) Km: Michaelis constant (Km = (k-1 + kcat)/k1 )
|
Table S2
Molecular name |
Full name |
Concentration |
References |
PKC |
Protein kinase C |
1 mM |
18 |
PP2A |
Protein phosphatase 2A |
0.045 mM |
19 |
Raf |
Raf |
0.5 mM |
20 |
MEK |
MAPK or ERK kinase |
0.5 mM |
21, 22 |
MAPK |
Mitogen-activated protein kinase |
1 mM |
22, 23 |
MKP |
MAPK phoaphatase |
0.0032 mM |
24 |
PLA2 |
Phospholipase A2 |
0.4 mM |
16 |
PIP2 |
Phosphatidylinositol bisphosphate |
10 mM |
4 |
APC |
Aracholonylphosphatidylcholine |
30 mM |
25 |
AMPAR |
AMPA receptor |
0.5 mM |
26 |
References for Table S1 and S2
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2. Schaechter, J. D., and Benowitz, L. I. (1993). Activation of protein kinase C by arachidonic acid selectively enhances the phosphorylation of GAP-43 in nerve terminal membranes. J Neurosci 13, 4361-4371.
3. Chen, S. J., Klann, E., Gower, M. C., Powell, C. M., Sessoms, J. S., and Sweatt, J. D. (1993). Studies with synthetic peptide substrates derived from the neuronal protein neurogranin reveal structural determinants of potency and selectivity for protein kinase C. Biochemistry 32, 1032-1039.
4. Kuroda, S., Schweighofer, N., and Kawato, M. (2001). Exploration of signal transduction pathways in cerebellar long-term depression by kinetic simulation. J Neurosci 21, 5693-5702.
5. Pato, M. D., Sutherland, C., Winder, S. J., and Walsh, M. P. (1993). Smooth-muscle caldesmon phosphatase is SMP-I, a type 2A protein phosphatase. Biochem J 293, 35–41.
6. Force, T., Bonventre, J. V., Heidecker, G., Rapp, U., Avruch, J., and Kyriakis, J. M. (1994). Enzymatic characteristics of the c-Raf-1 protein kinase. Proc Natl Acad Sci U S A 91, 1270-1274.
7. Kyriakis, J. M., App, H., Zhang, X. F., Banerjee, P., Brautigan, D. L., Rapp, U. R., and Avruch, J. (1992). Raf-1 activates MAP kinase-kinase. Nature 358, 417-421.
8. Ahn, S., Ginty, D. D., and Linden, D. J. (1999). A late phase of cerebellar long-term depression requires activation of CaMKIV and CREB. Neuron 23, 559-568.
9. Seger, R., Ahn, N. G., Posada, J., Munar, E. S., Jensen, A. M., Cooper, J. A., Cobb, M. H., and Krebs, E. G. (1992). Purification and characterization of mitogen-activated protein kinase activator(s) from epidermal growth factor-stimulated A431 cells. J Biol Chem 267, 14373-14381.
10. Haystead, T. A., Dent, P., Wu, J., Haystead, C. M., and Sturgill, T. W. (1992). Ordered phosphorylation of p42mapk by MAP kinase kinase. FEBS Lett 306, 17-22.
11. Charles, C. H., Abler, A. S., and Lau, L. F. (1992). cDNA sequence of a growth factor-inducible immediate early gene and characterization of its encoded protein. Oncogene 7, 187-190.
12. Charles, C. H., Sun, H., Lau, L. F., and Tonks, N. K. (1993). The growth factor-inducible immediate-early gene 3CH134 encodes a protein-tyrosine-phosphatase. Proc Natl Acad Sci U S A 90, 5292-5296.
13. Sanghera, J. S., Paddon, H. B., Bader, S. A., and Pelech, S. L. (1990). Purification and characterization of a maturation-activated myelin basic protein kinase from sea star oocytes. J Biol Chem 265, 52-57.
14. Nemenoff, R. A., Winitz, S., Qian, N. X., Van Putten, V., Johnson, G. L., and Heasley, L. E. (1993). Phosphorylation and activation of a high molecular weight form of phospholipase A2 by p42 microtubule-associated protein 2 kinase and protein kinase C. J Biol Chem 268, 1960-1964.
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16. Leslie, C. C., and Channon, J. Y. (1990). Anionic phospholipids stimulate an arachidonoyl-hydrolyzing phospholipase A2 from macrophages and reduce the calcium requirement for activity. Biochim Biophys Acta 1045, 261-270.
17. Channon, J. Y., and Leslie, C. C. (1990). A calcium-dependent mechanism for associating a soluble arachidonoyl-hydrolyzing phospholipase A2 with membrane in the macrophage cell line RAW 264.7. J Biol Chem 265, 5409-5413.
18. Marquez, C., Martinez, C., Kroemer, G., and Bosca, L. (1992). Protein kinase C isoenzymes display differential affinity for phorbol esters. Analysis of phorbol ester receptors in B cell differentiation. J Immunol 149, 2560-2568
19. Mumby, M. C., Green, D. D., and Russell, K., L. (1985). Structural characterization of cardiac protein phosphatase with a monoclonal antibody. Evidence that the Mr = 38,000 phosphatase is the catalytic subunit of the native enzyme(s). J Biol Chem 260, 13763-13770
20. Storm, S. M., Cleveland, J. L., and Rapp, U. R., (1990). Expression of raf family proto-oncogenes in normal mouse tissues. Oncogene 5, 345-351.
21. Seger, R., Ahn, N. G., Posada, J., Munar, E. S., Jensen, A. M., Cooper, J. A., Cobb, M. H., and Krebs, E. G. (1992). Purification and characterization of mitogen-activated protein kinase activator(s) from epidermal growth factor-stimulated A431 cells. J Biol Chem 267, 14373-14381.
22. Huang, C. Y., and Ferrell, J. E., Jr. (1996). Ultrasensitivity in the mitogen-activated protein kinase cascade. Proc Natl Acad Sci U S A 93, 10078-10083.
23. Sanghera, J. S., Paddon, H. B., Bader, S. A., and Pelech, S. L. (1990). Purification and characterization of a maturation-activated myelin basic protein kinase from sea star oocytes. J Biol Chem 265, 52-57.
24. Sun, H., Charles, C. H., Lau, L. F., and Tonks, N. K. (1993). MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo. Cell 75, 487-493.
25. Wijkander, J., and Sundler, R., (1991). An 100-kDa arachidonate-mobilizing phospholipase A2 in mouse spleen and the macrophage cell line J774. Purification, substrate interaction and phosphorylation by protein kinase C. Eur J Biochem 202, 873-880.
26. Tanaka, J., Matsuzaki, M., Tarusawa, E., Momiyama, A., Molnar, E., Kasai, H., and Shigemoto, R. (2005). Number and density of AMPA receptors in single synapses in immature cerebellum. J Neurosci 25, 799-807.