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.
Dupres, V., Alsteens, D., Wilk, S., Hansen, B., Heinisch, J. J., & Dufrêne, Y. (2009). The yeast Wsc1 cell surface sensor behaves like a nanospring in vivo. Nature Chemical Biology, 5(11), 857-862. https://doi.org/10.1038/nchembio.220 (Original work published 2009)