Diversification of CORVET tethers facilitates transport complexity in Tetrahymena thermophila

Daniela Sparvoli, Martin Zoltner, Chao-Yin Cheng, Mark C. Field, Aaron Turkewitz (Lead / Corresponding author)

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

In endolysosomal networks, two hetero-hexameric tethers called HOPS and CORVET are found widely throughout eukaryotes. The unicellular ciliate Tetrahymena thermophila possesses elaborate endolysosomal structures, but curiously both it and related protozoa lack the HOPS tether and several other trafficking proteins, while retaining the related CORVET complex. Here, we show that Tetrahymena encodes multiple paralogs of most CORVET subunits, which assemble into six distinct complexes. Each complex has a unique subunit composition and, significantly, shows unique localization, indicating participation in distinct pathways. One pair of complexes differ by a single subunit (Vps8), but have late endosomal versus recycling endosome locations. While Vps8 subunits are thus prime determinants for targeting and functional specificity, determinants exist on all subunits except Vps11. This unprecedented expansion and diversification of CORVET provides a potent example of tether flexibility, and illustrates how 'backfilling' following secondary losses of trafficking genes can provide a mechanism for evolution of new pathways.

Original languageEnglish
Article numberjcs238659
Pages (from-to)1-18
Number of pages18
JournalJournal of Cell Science
Volume133
Issue number3
Early online date21 Jan 2020
DOIs
Publication statusPublished - 12 Feb 2020

Keywords

  • Ciliates
  • Cryomilling
  • Endosomal trafficking
  • Evolutionary cell biology
  • Mass spectrometry
  • Paralogous expansion
  • Backfilling
  • CORVET
  • Ciliate

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