6f6p
From Proteopedia
Crystal structure of tetrameric human Rabin8 GEF domain
Structural highlights
FunctionRAB3I_HUMAN Guanine nucleotide exchange factor (GEF) which may activate RAB8A and RAB8B. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. Mediates the release of GDP from RAB8A and RAB8B but not from RAB3A or RAB5. Modulates actin organization and promotes polarized transport of RAB8A-specific vesicles to the cell surface. Together with RAB11A, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis.[1] [2] [3] Publication Abstract from PubMedRab GTPases and their effectors, activators and guanine nucleotide exchange factors (GEFs) are essential for vesicular transport. Rab8 and its GEF Rabin8 function in formation of the cilium organelle important for developmental signaling and sensory reception. Here we show by size exclusion chromatography and analytical ultracentrifugation that Rabin8 exists in equilibrium between dimers and tetramers. The crystal structure of tetrameric Rabin8 GEF domain reveals an occluded Rab8 binding site suggesting that this oligomer is enzymatically inactive, a notion we verify experimentally using Rabin8/Rab8 GEF assays. We outline a procedure for the purification of active dimeric Rabin8 GEF-domain for in vitro activity assays. This article is protected by copyright. All rights reserved. Crystal structure of tetrameric human Rabin8 GEF domain.,Vetter M, Boegholm N, Christensen A, Bhogaraju S, Andersen MB, Lorentzen A, Lorentzen E Proteins. 2018 Jan 10. doi: 10.1002/prot.25455. PMID:29318657[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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