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Fig. 10. Diagram of the mechanism controlling nucleostemin distribution between the nucleolar and nucleoplasmic compartments, and the effects of RSL1D1 knockdown and nlsL1 overexpression. Nucleostemin in the GTP-unbound state is blocked from entering the nucleolus by a nucleoplasmic-retaining mechanism that acts on the I-domain. GTP binding releases this lock and allows nucleostemin to move into the nucleolus. Nucleostemin interacts with nucleolar protein RSL1D1 through the nucleolus-targeting B- and G-domains. When not bound by GTP, the GI-domain fails to interact with RSL1D1, suggesting a link between the nucleolar exit of nucleostemin and GTP hydrolysis. RSL1D1 co-resides with nucleostemin in subnucleolar domains surrounding fibrillarin. A partial knockdown of RSL1D1 expression reduces the compartmental size and, to a lesser extent, the protein amount of nucleostemin in the nucleolus, supporting the idea that RSL1D1 provides the nucleolar binding site for nucleostemin. Overexpression of nlsL1 disperses nucleostemin signals from the nucleolus by occupying the nucleolar binding sites for the endogenous RSL1D1 capable of interacting with nucleostemin. NoLS, nucleolar localization sequence(s); NOR, nucleolar organization region; Fib, fibrillarin.

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