Identical domains of Yarrowia lipolytica Vps23 are required for both ESCRT and Rim pathways, but the latter needs an interaction between the Vps23 UEV domain and Rim8/PalF

FEMS Yeast Res. 2011 Sep;11(6):473-86. doi: 10.1111/j.1567-1364.2011.00735.x. Epub 2011 May 23.

Abstract

A conserved pathway, called Rim or Pal, transduces the ambient pH signal in ascomycetous yeasts and fungi, respectively. This pathway requires most of the components of the endosomal sorting complex required for transport (ESCRT) pathway. In the yeast Yarrowia lipolytica, a functional analysis of the ESCRT-I subunit Vps23 was carried out by in-frame deletions of each of the conserved domains to test whether Vps23 functions in the Rim and ESCRT pathways could be separated. These two pathways were shown to necessitate both the coiled-coil domain and the C-terminal steadiness box. However, the central proline-rich region seems to be required for neither of them. Both pathways involve the N-terminal ubiquitin E2 variant (UEV) domain. Thus, identical domains of YlVps23 are required for both Rim and ESCRT pathways, but the UEV domain was shown to bind the arrestin-like protein Rim8/PalF in the Rim pathway, whereas it binds Vps27 in the ESCRT pathway. Vps23 is therefore required to link pH signalling and endocytosis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • DNA Mutational Analysis
  • Endocytosis
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism*
  • Hydrogen-Ion Concentration
  • Protein Binding
  • Protein Interaction Domains and Motifs
  • Protein Interaction Mapping
  • Sequence Deletion
  • Signal Transduction*
  • Stress, Physiological
  • Yarrowia / genetics
  • Yarrowia / metabolism*

Substances

  • Fungal Proteins