Abstract
Microtubules are highly dynamic filaments assembled from αβ-tubulin heterodimers and play important roles in many cellular processes, including cell division and migration. Microtubule dynamics is tightly regulated by microtubule-associated proteins (MAPs) that function by binding to microtubules or free tubulin dimers. Here, we report that FOR20 (FOP-related protein of 20 kDa), a conserved protein critical for ciliogenesis and cell cycle progression, is a previously uncharacterized MAP that facilitates microtubule depolymerization and promotes cell migration. FOR20 not only directly binds to microtubules but also regulates microtubule dynamics in vitro by decreasing the microtubule growth rate and increasing the depolymerization rate and catastrophe frequency. In the in vitro microtubule dynamics assays, FOR20 appears to preferentially interact with free tubulin dimers over microtubules. Depletion of FOR20 inhibits microtubule depolymerization and promotes microtubule regrowth after the nocodazole treatment in HeLa cells. In addition, FOR20 knockdown significantly inhibits both individual and collective migration of mammalian cells. Taken together, these data suggest that FOR20 functions as a MAP to promote microtubule depolymerization and cell migration.
Highlights
Microtubules have pivotal roles in fundamental cellular processes, such as cell division, intracellular transport and cell migration [1, 2]
We investigated cellular microtubule dynamics in cells treated with nocodazole and FOR20 depletion, and discovered that knockdown of FOR20 significantly retarded microtubule depolymerization induced by nocodazole (Figure 6c and d)
FOR20 is essential for cell migration Given that microtubule dynamics is required for cell motility [1, 4], we tested if FOR20 has a role in cell
Summary
Microtubules have pivotal roles in fundamental cellular processes, such as cell division, intracellular transport and cell migration [1, 2] They are highly dynamic filaments assembled from αβ-tubulin heterodimers [3,4,5,6]. GTP bound to βtubulin makes microtubules more prone to polymerization, whereas microtubules with GDP bound to βtubulin tend to depolymerize [4]. The antitumor drug taxol interacts with and stabilizes microtubules by preventing microtubule depolymerization even in the absence of exogenous GTP [8,9,10]. Microtubule dynamics is tightly regulated (that is, stabilizing or destabilizing) by microtubuleassociated proteins (MAPs) that act by binding to the microtubule lattice or free tubulin dimers [11,12,13]
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