The Sur7 cytoplasmic C terminus regulates morphogenesis and stress responses in Candida albicans

Mol Microbiol. 2021 Oct;116(4):1201-1215. doi: 10.1111/mmi.14806. Epub 2021 Sep 15.

Abstract

MCC/eisosome subdomains of the plasma membrane promote proper cell wall morphogenesis that is critical for the fungal pathogen Candida albicans to grow invasively and resist stressful environments in the host. Sur7 localizes to MCC/eisosomes and is needed for their function, so in this work, the role of this tetraspan membrane protein was studied by mutagenesis. Deletion mutant analysis showed that the N-terminal region containing the four transmembrane domains mediates Sur7 localization to MCC/eisosomes. Mutation of 32 conserved residues in the N-terminal region indicated that extracellular loop 1 is important, although these mutants generally displayed weak phenotypes. Surprisingly, two Cys residues in a conserved motif in extracellular loop 1 were not important. However, deletion of the entire 15 amino acid motif revealed that it was needed for proper membrane trafficking of Sur7. Deletion and substitution mutagenesis showed that the C terminus is important for resisting cell wall stress. This is significant as it indicates Sur7 carries out an important role in the cytoplasm. Altogether, these results indicate that the N-terminal region localizes Sur7 to MCC/eisosomes and that the C-terminal domain promotes responses in the cytoplasm needed for cell wall morphogenesis and stress resistance.

Keywords: MCC; Sur7; eisosome; fungal; membrane domain; stress resistance; tetraspan protein.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Motifs
  • Candida albicans / genetics*
  • Candida albicans / metabolism*
  • Cell Membrane / metabolism
  • Cell Wall / metabolism
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism
  • Humans
  • Membrane Proteins / genetics*
  • Membrane Proteins / metabolism*
  • Morphogenesis*
  • Sequence Deletion
  • Stress, Physiological*

Substances

  • Fungal Proteins
  • Membrane Proteins