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Commentary

Interactions between Rab and Arf GTPases regulate endosomal phosphatidylinositol-4,5-bisphosphate during endocytic recycling

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Pages 106-109 | Received 17 Oct 2012, Accepted 03 Jan 2013, Published online: 07 Feb 2013

Figures & data

Figure 1. Coordinate Rab/Arf GTPase cascades influence multiple cellular processes. (A) In C. elegans, RAB-10 and ARF-6 act in sequential steps via CNT-1/Arf GAP to regulate endosomal PI(4,5)P2 levels and membrane recruitment of recycling traffic related PI(4,5)P2-binding proteins RME-1 and SDPN-1. (B) In mammalian systems, Rab35(GTP) recruits ACAP2/Arf GAP and thus regulates Arf6 activity. Rab35-mediated regulation of Arf6 via ACAP2 is important for NGF-induced outgrowth of neurite and phagocytosis. Recent studies suggested that Arf6 can recruit MICAL-L1 onto endosomes and regulate EHD1 and Rab8 localization/function indirectly. Arf6(GTP) also interacts with the Rab35 GAP EPI64B, negatively regulating Rab35 activity. This Arf6-to-Rab35 cascade is necessary for endocytic trafficking during cytokinesis.

Figure 1. Coordinate Rab/Arf GTPase cascades influence multiple cellular processes. (A) In C. elegans, RAB-10 and ARF-6 act in sequential steps via CNT-1/Arf GAP to regulate endosomal PI(4,5)P2 levels and membrane recruitment of recycling traffic related PI(4,5)P2-binding proteins RME-1 and SDPN-1. (B) In mammalian systems, Rab35(GTP) recruits ACAP2/Arf GAP and thus regulates Arf6 activity. Rab35-mediated regulation of Arf6 via ACAP2 is important for NGF-induced outgrowth of neurite and phagocytosis. Recent studies suggested that Arf6 can recruit MICAL-L1 onto endosomes and regulate EHD1 and Rab8 localization/function indirectly. Arf6(GTP) also interacts with the Rab35 GAP EPI64B, negatively regulating Rab35 activity. This Arf6-to-Rab35 cascade is necessary for endocytic trafficking during cytokinesis.

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