Figure 6. Rab18 binds to NRZ tethering complex. (A) Rab18 interacted with NRZ complex. (B and C) Rab18 interacted with ZW10. (D) ZW10 interacted with GTP-bound Rab18 in vitro with a higher affinity. (E) ZW10 enhanced the interaction between Rab18 and NAG. Right: Schematic diagram showing the interaction pattern between Rab18 and NRZ complex. (F) The LD association of NAG and ZW10 was dependent on Rab18. Subcellular fractions were isolated from control or Rab18-deficient TM-3 cells. ADRP, GRP94, GM130, and β-tubulin represent LD, microsomal, Golgi, and cytosolic markers, respectively. (G) Colocalization of HA-Rab18 (pink), Cherry-ZW10 (red), and endogenous NAG (green) on LDs (blue). Bars: 10 µm; (insets) 2 µm. (H) Association of endogenous ZW10 (green) or endogenous NAG (green) with LDs (blue) in the presence of Rab18 (red). Bars: 10 µm; (insets) 2 µm. All experiments were performed at least twice. FL, full-length.
Figure 6.

Rab18 binds to NRZ tethering complex. (A) Rab18 interacted with NRZ complex. (B and C) Rab18 interacted with ZW10. (D) ZW10 interacted with GTP-bound Rab18 in vitro with a higher affinity. (E) ZW10 enhanced the interaction between Rab18 and NAG. Right: Schematic diagram showing the interaction pattern between Rab18 and NRZ complex. (F) The LD association of NAG and ZW10 was dependent on Rab18. Subcellular fractions were isolated from control or Rab18-deficient TM-3 cells. ADRP, GRP94, GM130, and β-tubulin represent LD, microsomal, Golgi, and cytosolic markers, respectively. (G) Colocalization of HA-Rab18 (pink), Cherry-ZW10 (red), and endogenous NAG (green) on LDs (blue). Bars: 10 µm; (insets) 2 µm. (H) Association of endogenous ZW10 (green) or endogenous NAG (green) with LDs (blue) in the presence of Rab18 (red). Bars: 10 µm; (insets) 2 µm. All experiments were performed at least twice. FL, full-length.

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