Fig. 8: Schematic summary of the role played by nuclear-capture of EphA2 endosomes in controlling nuclear G-actin dynamics. | Nature Communications

Fig. 8: Schematic summary of the role played by nuclear-capture of EphA2 endosomes in controlling nuclear G-actin dynamics.

From: Nuclear-capture of endosomes depletes nuclear G-actin to promote SRF/MRTF activation and cancer cell invasion

Fig. 8

MET drives clathrin and Rab17-dependent endocytosis of EphA2 [1]. EphA2/Rab17-positive endosomes are then transported centripetally [2] and become physically attached to, or ‘captured’ by, the nucleus by an interaction formed between the nuclear import machinery and a nuclear localization sequence located in EphA2’s cytodomain [3]. This nuclear-capture event, in turn, drives actin polymerization, which is restricted to the juxta-nuclear region [4] and LIMK-driven phosphorylation of cofilin [5], and both events are dependent on the RhoG GTPase. Phosphorylation of cofilin opposes nuclear import of cofilin–actin, leading to depletion of G-actin from the nucleus [6], which, in turn, activates transcription of MRTF/SRF target genes [7] to implement cell scattering and invasion.

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