The yeast Wsc1 cell surface sensor behaves like a nanospring in vivo

Nat Chem Biol. 2009 Nov;5(11):857-62. doi: 10.1038/nchembio.220. Epub 2009 Sep 20.


Here we report on in vivo measurement of the mechanical behavior of a cell surface sensor using single-molecule atomic force microscopy. We focus on the yeast wall stress component sensor Wsc1, a plasma membrane protein that is thought to function as a rigid probe of the cell wall status. We first map the distribution of individual histidine-tagged sensors on living yeast cells by scanning the cell surface with atomic force microscopy tips carrying nitrilotriacetate groups. We then show that Wsc1 behaves like a linear nanospring that is capable of resisting high mechanical force and of responding to cell surface stress. Both a genomic pmt4 deletion and the insertion of a stretch of glycines in Wsc1 result in substantial alterations in protein spring properties, supporting the important role of glycosylation at the extracellular serine/threonine-rich region.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biosensing Techniques*
  • Cell Membrane / physiology*
  • Cell Membrane / ultrastructure
  • Cell Wall / physiology
  • Cell Wall / ultrastructure
  • Cells, Immobilized / physiology
  • Cells, Immobilized / ultrastructure
  • Intracellular Signaling Peptides and Proteins / chemistry
  • Intracellular Signaling Peptides and Proteins / physiology
  • Membrane Glycoproteins / chemistry
  • Membrane Glycoproteins / physiology
  • Membrane Proteins / physiology
  • Membrane Proteins / ultrastructure
  • Microscopy, Atomic Force / methods*
  • Models, Molecular
  • Protein Conformation
  • Saccharomyces cerevisiae / physiology*
  • Saccharomyces cerevisiae / ultrastructure
  • Saccharomyces cerevisiae Proteins / chemistry
  • Saccharomyces cerevisiae Proteins / physiology
  • Saccharomyces cerevisiae Proteins / ultrastructure
  • Solutions
  • Stress, Mechanical


  • Intracellular Signaling Peptides and Proteins
  • MID2 protein, S cerevisiae
  • Membrane Glycoproteins
  • Membrane Proteins
  • SLG1 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Solutions