Modeling protein dynamics in Caenorhabditis elegans embryos reveals that the PLK-1 gradient relies on weakly coupled reaction-diffusion mechanisms

Proc Natl Acad Sci U S A. 2022 Mar 15;119(11):e2114205119. doi: 10.1073/pnas.2114205119. Epub 2022 Mar 8.

Abstract

SignificanceIntracellular gradients have essential roles in cell and developmental biology, but their formation is not fully understood. We have developed a computational approach facilitating interpretation of protein dynamics and gradient formation. We have combined this computational approach with experiments to understand how Polo-Like Kinase 1 (PLK-1) forms a cytoplasmic gradient in Caenorhabditis elegans embryos. Although the PLK-1 gradient depends on the Muscle EXcess-5/6 (MEX-5/6) proteins, we reveal differences in PLK-1 and MEX-5 gradient formation that can be explained by a model with two components, PLK-1 bound to MEX-5 and unbound PLK-1. Our combined approach suggests that a weak coupling between PLK-1 and MEX-5 reaction-diffusion mechanisms dictates the dynamic exchange of PLK-1 with the cytoplasm, explaining PLK-1 high diffusivity and smooth gradient.

Keywords: MEX-5; computational modeling; intracellular gradient establishment; polo-like kinase 1; reaction–diffusion mechanisms.

MeSH terms

  • Animals
  • Caenorhabditis elegans / embryology*
  • Caenorhabditis elegans / metabolism*
  • Caenorhabditis elegans Proteins / metabolism*
  • Embryo, Nonmammalian
  • Models, Biological
  • Monte Carlo Method
  • Morphogenesis
  • Protein Serine-Threonine Kinases
  • Protein Transport
  • Proteome*
  • Proteomics* / methods

Substances

  • Caenorhabditis elegans Proteins
  • MEX-5 protein, C elegans
  • Proteome
  • Protein Serine-Threonine Kinases
  • plk-1 protein, C elegans