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Autophagic punctum

The C9orf72-SMCR8-WDR41 complex is a GAP for small GTPases

, , , & ORCID Icon
Pages 1542-1543 | Received 05 May 2020, Accepted 26 May 2020, Published online: 17 Jun 2020

Figures & data

Figure 1. Model of the CSW complex. (A) The overall structure of the CSW complex. The structure shows a two-fold symmetry. C9orf72, SMCR8, and WDR41 are colored in light blue, light green, and orange, respectively. The domains are denoted. The arginine finger is highlighted in red dashed lines. The dimer interface of the two protomers is denoted in blue dashed lines. (B) The proposed model of how the CSW complex promotes the fusion of endosomes: the CSW complex tethers two endosomes using WDR41, and promotes the fusion by activating RABs located on the surface of endosomes. C9orf72, SMCR8, and WDR41 are colored in blue, green, and yellow, respectively, while RABs are shown in dark blue. The arginine finger is highlighted as a dark pink line. The organization of domains is based on the structure in (A).

Figure 1. Model of the CSW complex. (A) The overall structure of the CSW complex. The structure shows a two-fold symmetry. C9orf72, SMCR8, and WDR41 are colored in light blue, light green, and orange, respectively. The domains are denoted. The arginine finger is highlighted in red dashed lines. The dimer interface of the two protomers is denoted in blue dashed lines. (B) The proposed model of how the CSW complex promotes the fusion of endosomes: the CSW complex tethers two endosomes using WDR41, and promotes the fusion by activating RABs located on the surface of endosomes. C9orf72, SMCR8, and WDR41 are colored in blue, green, and yellow, respectively, while RABs are shown in dark blue. The arginine finger is highlighted as a dark pink line. The organization of domains is based on the structure in (A).

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