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Characterisation of the Ubiquitin-ESCRT pathway in Asgard archaea sheds new light on origins of membrane trafficking in eukaryotes

Research output: Contribution to Journal/MagazineJournal article

  • Tomoyuki Hatano
  • Saravanan Palani
  • Dimitra Papatziamou
  • Diorge Souza
  • Ralf Salzer
  • Daniel Tamarit
  • Mehul Makwana
  • Antonia Potter
  • Alexandra Haig
  • Wenjue Xu
  • David Townsend
  • David Rochester
  • Dom Bellini
  • Hamdi Hussain
  • Thijs Ettema
  • Jan Löwe
  • Buzz Baum
  • Nick Robinson
  • Mohan Balasubramanian
<mark>Journal publication date</mark>17/08/2021
Number of pages27
Publication StatusPublished
<mark>Original language</mark>English


The ESCRT machinery performs a critical role in membrane remodelling events in all eukaryotic cells, including in membrane trafficking, membrane repair, cytokinetic abscission, in viral egress, and in the generation of extracellular vesicles. While the machinery is complex in modern day eukaryotes, where it comprises dozens of proteins, the system has simpler and more ancient origins. Indeed, homologues of ESCRT-III and the Vps4 ATPase, the proteins that execute the final membrane scission reaction, play analogous roles in cytokinesis and potentially in extracellular vesicle formation in TACK archaea where ESCRT-I and II homologues seem to be absent. Here, we explore the phylogeny, structure, and biochemistry of homologues of the ESCRT machinery and the associated ubiquitylation system found in genome assemblies of the recently discovered Asgard archaea. In these closest living prokaryotic relatives of eukaryotes, we provide evidence for the ESCRT-I and II sub-complexes being involved in the ubiquitin-directed recruitment of ESCRT-III,_as it is in eukaryotes. This analysis suggests a pre-eukaryotic origin for the Ub-coupled ESCRT system and a likely path of ESCRT evolution via a series of gene duplication and diversification events.