Interaction of actin filaments with microtubules is mediated by microtubule-associated proteins and regulated by phosphorylation.
We have reconstituted high viscosity networks of actin filaments and microtubules from purified actin, tubulin, and MAPs. MAP-2 can effectively cross-link actin filaments and microtubules, presumably because a low affinity actin binding site is available even when it is bound tightly to microtubules. Phosphorylation of MAP-2 inhibits cross-linking of actin filaments and microtubules. Tau is not an effective cross-linker of actin and microtubules even though it can interact with each polymer individually.
Selden
S C
SC
Pollard
T D
TD
D008841:Actin Cytoskeleton / Q000378:metabolism* / Q000648:ultrastructure; D000199:Actins / Q000378:metabolism*; D000818:Animals; D001921:Brain / Q000378:metabolism; D003599:Cytoskeleton / Q000378:metabolism*; D007700:Kinetics; D046911:Macromolecular Substances; D008869:Microtubule-Associated Proteins / Q000378:metabolism*; D008870:Microtubules / Q000378:metabolism* / Q000648:ultrastructure; D009132:Muscles / Q000378:metabolism; D010766:Phosphorylation; D011817:Rabbits; D013552:Swine; D014783:Viscosity
D000199:Actins; D046911:Macromolecular Substances; D008869:Microtubule-Associated Proteins