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Interaction of Actin Filaments with Microtubules Is Mediated by Microtubule‐Associated Proteins and Regulated by Phosphorylation a
Author(s) -
SELDEN S. CHARLES,
POLLARD THOMAS D.
Publication year - 1986
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1986.tb38464.x
Subject(s) - annals , citation , library science , medicine , classics , computer science , art
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.