Table 4.

Parameters and initial conditions for the fitting

Row Parameters (unit) Setting Initial value of TRPC6 endo/C6 + M1R/A7r5/C7 + M1Source or comments 
PI(4,5)P2 (µM) at resting Free 20/20/20/20 Bunce et al., 1993; McLaughlin and Murray, 2005  
ki_PLC (s−1Free 0.04/1/1/1 Rational to PI(4,5)P2 reduction with our data 
kii_DAG kinase (s−1Free 0.03/0.03/0.08/0.03 Rational to DAG changes with our data 
kiii_PA to PIP reactions (s−1Free 0.01/0.01/0.01/0.01 Appropriate for PI(4,5)P2 synthesis 
kiv_PIP5K (s−1Free 0.1/0.1/0.25/0.1 Appropriate for PI(4,5)P2 resynthesis 
kv_IP3 phosphatase (s−1Free 0.5/0.5/0.5/0.5 Appropriate for IP3 hydrolysis 
τrd (s) Free 5/2/1/4 Appropriate for Receptor desensitization 
τsd (s) Free 50/10/5/10 Same as above 
Rd_f (no unit) Free 0.5/0.5/0.5/0.5 Same as above 
10 Sd_f (no unit) Free 0.5/0.5/0.5/0.5 Same as above 
11 spot (distance global to local; µm) Free 4/4/3/4 5 times more than the diffusion coefficient of PI(4,5)P2 
12 dcoef of PI(4,5)P2 (µm2/s) Free 0.8/0.8/0.8/0.8 Golebiewska et al., 2008  
13 Ratio of local ki / global ki Free 1/4/2/5 Approximate from the uneven FRET reduction (Fig. S3) 
14 PI4P (µM) Fixed 10/10/10/10 Brown et al., 2008  
15 Activation delay (no unit) Free 0.01/0.001/0.001/0.001 Appropriate for receptor activation 
16 Activation power (no unit) Free 0.5/0.3/0.7/0.3 Same as above 
17 Vrev (mV) Fixed 0/0/0/0  
18 Vhold (mV) Fixed −50/−50/−50/−50  
19 No. of channels Free 100–7,000 Appropriate for the current density 
20 Channel conductance (pS) Fixed 35/35/35/70 Hofmann et al., 1999; Lemonnier et al., 2008  
21 K1 (Kd for DAG1; µM) Free 60/60/35/10 Effective OAG concentrations are 10 to 100 µM in Hofmann et al., 1999; Okada et al., 1999; Imai et al., 2012  
22 K2 (Kd for DAG2; µM) Free 30/30/10/10 Same as above 
23 K3 (Kd for PI(4,5)P2; µM) Free 2/2/5/5 This paper, Fig. 4 D  
24 Expressed PHd (µM) Fixed 1.6/1.6/1.6/1.6 This paper, Materials and methods 
25 Kd PI(4,5)P2 of PHd (µM) Fixed 2.0/2.0/2.0/2.0 Hirose et al., 1999  
26 Kd IP3 of PHd (µM) Fixed 0.1/0.1/0.1/0.1 Hirose et al., 1999  
Row Parameters (unit) Setting Initial value of TRPC6 endo/C6 + M1R/A7r5/C7 + M1Source or comments 
PI(4,5)P2 (µM) at resting Free 20/20/20/20 Bunce et al., 1993; McLaughlin and Murray, 2005  
ki_PLC (s−1Free 0.04/1/1/1 Rational to PI(4,5)P2 reduction with our data 
kii_DAG kinase (s−1Free 0.03/0.03/0.08/0.03 Rational to DAG changes with our data 
kiii_PA to PIP reactions (s−1Free 0.01/0.01/0.01/0.01 Appropriate for PI(4,5)P2 synthesis 
kiv_PIP5K (s−1Free 0.1/0.1/0.25/0.1 Appropriate for PI(4,5)P2 resynthesis 
kv_IP3 phosphatase (s−1Free 0.5/0.5/0.5/0.5 Appropriate for IP3 hydrolysis 
τrd (s) Free 5/2/1/4 Appropriate for Receptor desensitization 
τsd (s) Free 50/10/5/10 Same as above 
Rd_f (no unit) Free 0.5/0.5/0.5/0.5 Same as above 
10 Sd_f (no unit) Free 0.5/0.5/0.5/0.5 Same as above 
11 spot (distance global to local; µm) Free 4/4/3/4 5 times more than the diffusion coefficient of PI(4,5)P2 
12 dcoef of PI(4,5)P2 (µm2/s) Free 0.8/0.8/0.8/0.8 Golebiewska et al., 2008  
13 Ratio of local ki / global ki Free 1/4/2/5 Approximate from the uneven FRET reduction (Fig. S3) 
14 PI4P (µM) Fixed 10/10/10/10 Brown et al., 2008  
15 Activation delay (no unit) Free 0.01/0.001/0.001/0.001 Appropriate for receptor activation 
16 Activation power (no unit) Free 0.5/0.3/0.7/0.3 Same as above 
17 Vrev (mV) Fixed 0/0/0/0  
18 Vhold (mV) Fixed −50/−50/−50/−50  
19 No. of channels Free 100–7,000 Appropriate for the current density 
20 Channel conductance (pS) Fixed 35/35/35/70 Hofmann et al., 1999; Lemonnier et al., 2008  
21 K1 (Kd for DAG1; µM) Free 60/60/35/10 Effective OAG concentrations are 10 to 100 µM in Hofmann et al., 1999; Okada et al., 1999; Imai et al., 2012  
22 K2 (Kd for DAG2; µM) Free 30/30/10/10 Same as above 
23 K3 (Kd for PI(4,5)P2; µM) Free 2/2/5/5 This paper, Fig. 4 D  
24 Expressed PHd (µM) Fixed 1.6/1.6/1.6/1.6 This paper, Materials and methods 
25 Kd PI(4,5)P2 of PHd (µM) Fixed 2.0/2.0/2.0/2.0 Hirose et al., 1999  
26 Kd IP3 of PHd (µM) Fixed 0.1/0.1/0.1/0.1 Hirose et al., 1999  

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