Skip to main content
. 2021 Apr 19;32(9):869–879. doi: 10.1091/mbc.E20-11-0723

TABLE 1:

Summary of microtubule-associated proteins (MAPs) that may slow down plus-end depolymerization rate.

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.