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• W2892366841 abstract "Protein concentration gradients are a common strategy to compartmentalize activities within cells and tissues. Gradients position the division plane of bacterial cells, regulate the size of yeast cells, and pattern embryos (1⇓–3). Among the most studied gradients is the Bicoid gradient of Drosophila . Bicoid protein is synthesized from a localized source of bcd mRNA at the anterior-most pole of the embryo (4, 5). In one model, newly synthesized Bicoid is proposed to diffuse away from this point source and to turn over at a constant rate throughout the cytoplasm, thus generating an anterior-rich protein concentration gradient (6) (Fig. 1 A ). Drosophila embryos, however, are unusually large (>400 μm) syncytial cells. Smaller cells are unlikely to support Bicoid-like gradients, since the rate of protein diffusion in the cytoplasm is typically too fast (10 μm2⋅s−1) to prevent proteins from sampling the entire cytoplasm within seconds (2, 7). If so, how do most cells generate protein gradients? In 2008, Lipkow and Odde (8) offered a simple solution to this dilemma. Using theoretical modeling, they demonstrated that protein gradients can be sustained in cells of any size by coupling regulation of protein diffusivity to a spatially segregated protein modification system. The reversible protein modification (e.g., phosphorylation) toggles the protein between two states with different diffusion coefficients (one fast and one slow). Imposing a spatial bias in the distribution of one of the protein modification enzymes (e.g., the kinase) locally increases the concentration of one diffusive state, thus generating a protein concentration gradient whose steepness is proportional to the amplitude of the difference in protein diffusion coefficients (8). In PNAS, Wu et al. (9) provide remarkable experimental evidence that such a mechanism drives the formation of cytoplasmic gradients in … [↵][1]1To whom correspondence should be addressed. Email: gseydoux{at}jhmi.edu. [1]: #xref-corresp-1-1" @default.
• W2892366841 created "2018-09-27" @default.
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• W2892366841 date "2018-09-04" @default.
• W2892366841 modified "2023-10-16" @default.
• W2892366841 title "Single-molecule study reveals the frenetic lives of proteins in gradients" @default.
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• W2892366841 doi "https://doi.org/10.1073/pnas.1812248115" @default.
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