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. 1986:466:803-12.
doi: 10.1111/j.1749-6632.1986.tb38464.x.

Interaction of actin filaments with microtubules is mediated by microtubule-associated proteins and regulated by phosphorylation

S C Selden, T D Pollard

Interaction of actin filaments with microtubules is mediated by microtubule-associated proteins and regulated by phosphorylation

S C Selden et al. Ann N Y Acad Sci. 1986.

Abstract

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.

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