Journal
DEVELOPMENTAL CELL
Volume 42, Issue 4, Pages 416-+Publisher
CELL PRESS
DOI: 10.1016/j.devcel.2017.07.024
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Funding
- NIH Office of Research Infrastructure Programs [P40 OD010440]
- NIH [T32 CA009156, K99 GM115964, R01 GM083071]
- Howard Hughes post-doctoral fellowship from the Helen Hay Whitney Foundation
- SNF [31003A_138501, 31003A_156013]
- University of Geneva
- French Medical Research Foundation Equipe FRM [DEQ20140329538]
- Swiss National Science Foundation (SNF) [31003A_138501, 31003A_156013] Funding Source: Swiss National Science Foundation (SNF)
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Regulated protein-protein interactions are critical for cell signaling, differentiation, and development. For the study of dynamic regulation of protein interactions in vivo, there is a need for techniques that can yield time-resolved information and probe multiple protein binding partners simultaneously, using small amounts of starting material. Here we describe a single-cell protein interaction assay. Single-cell lysates are generated at defined time points and analyzed using single-moleculepull-down, yielding information about dynamic protein complex regulation in vivo. We established the utility of this approach by studying PAR polarity proteins, which mediate polarization of many animal cell types. We uncovered striking regulation of PAR complex composition and stoichiometry during Caenorhabditis elegans zygotepolarization, which takes place in less than 20 min. PAR complex dynamics are linked to the cell cycle by Polo-like kinase 1 and govern the movement of PAR proteins to establish polarity. Our results demonstrate an approach to study dynamic biochemical events in vivo.
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