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. Author manuscript; available in PMC: 2022 Jun 16.
Published in final edited form as: Neuron. 2021 May 24;109(12):1963–1978.e5. doi: 10.1016/j.neuron.2021.04.021

Figure 5. Recruitment of cargo proteins into Rapsn condensates.

Figure 5.

(A) Schematic domain structure of Rapsn and interaction proteins.

(B, C) AChR-α, AChR-β, MACF1, β-dystroglycan, α-actinin or calpain, but not GST, LRP4, or actin, were recruited into Rapsn LLPS-mediated condensates.

(D) FRAP analysis of AChR-α and α-actinin enriched in Rapsn droplets showing dynamic protein exchange.

(E) Quantification of fluorescence recovery of AChR-α and α-actinin in (D).

(F) Recruitment of actin into Rapsn condensed droplets in the presence of α-actinin.

(G) Quantification of the pixel ratio of CF633 / Rapsn-EGFP in (F).

Data was shown as mean ± SEM; n = or > 3.

See also Figures S4 and S5.