Nogo-66, a potent inhibitory domain of Nogo, signals through a tripartite Nogo receptor complex on neurons that leads to growth cone collapse and neurite outgrowth inhibition through cytoskeletal rearrangement. Here, we indicate that cofilin is one of the actin-binding proteins regulated by Nogo-66 under the influence of Rho GTPases. We observed a sequential change of cofilin phosphorylation from 0 to 60 minutes after Nogo-66 treatment. The increase and decrease of cofilin phosphorylation induced by Nogo-66 is regulated by LIMK1 and SSH1L, respectively. Both LIMK1 and SSH1L activity are regulated by Nogo-66 in a ROCK-dependent manner. 14-3-3 proteins are cytosolic scaffolding proteins that mediate Nogo-66 signals toward cofilin through interacting with SSH1L phosphatase.

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