TABLE 1:
Gene symbol | Protein description | Abundance (nM) | Kd (nM) | Reference | θ at low P | θ at P = 1.6 µM | θ fold change |
---|---|---|---|---|---|---|---|
MAP4 | Microtubule-associated protein, XMAP230 | 964.5 | 300 | Tokuraku et al., 2003; Andersen et al., 1994 | 0.76 | 0.45 | 1.69 |
EML2 | Echinoderm microtubule-associated protein-like 2 | 578.18 | ? | ||||
EML4 | EML4 protein | 504.2 | 180 | Eichenmuller et al., 2001 | 0.74 | 0.27 | 2.74 |
EML1 | Echinoderm microtubule-associated protein-like 1 | 135.67 | ? | ||||
MAP7 | Ensconsin | 91.3 | 460 | Monroy et al., 2020 | 0.17 | 0.04 | 4.25 |
MAP1B | Microtubule-associated protein 1B, XMAP310 | 84.68 | 200 | Andersen and Karsenti, 1997 | 0.3 | 0.05 | 6.0 |
MAP1S | MAP1S light chain | 66.04 | ? | ||||
MAP7D1 | MAP7 domain-containing protein 1 | 46.97 | ? | ||||
MAP7D2 | MAP7 domain-containing 2 protein variant 2 (fragment) | 8.55 | ? |
Protein abundance in the frog egg is from proteome data in Wühr et al. (2014). For those with reported dissociation constants (Andersen et al., 1994; Andersen and Karsenti, 1997; Eichenmüller et al., 2001; Tokuraku et al., 2003; Monroy et al. 2020), we provide the estimated value of θ, the fractional occupancy of the microtubule lattice at low (i.e., excess MAP) and high polymer concentrations (P = 1.6 µM). See Supplemental Table 1 for an extended list of MAPs.