@article {69796,
	title = {BPS2025 - Local cytoplasmic tradewinds direct soluble proteins to their targets},
	journal = {Biophysical Journal},
	volume = {124},
	year = {2025},
	month = {2025 Feb 13},
	pages = {375a - 376a},
	abstract = {<p>Inside the cell, proteins essential for signaling, morphogenesis, and migration navigate the complex, ever-changing environment through vesicular trafficking or microtubule-driven mechanisms. However, the mechanisms by which soluble proteins reach their target destinations remain unknown. Here, we show that soluble proteins are directed toward the cell{\textquoteright}s advancing edge by advection, diffusion facilitated by fluid flow. The advective transport mechanism operates in a compartment at the front of the cell isolated from the rest of the cytoplasm by a semi-permeable actin-myosin barrier that restricts protein mixing between the compartment and the rest of the cytoplasm. Contraction at the barrier generates a molecularly non-specific fluid flow that propels treadmilling actin monomer, actin-binding, adhesion, and even inert proteins forward. Changes in the dynamic local curvature of the barrier direct the flow, targeting proteins toward the protruding regions of the leading edge, effectively coordinating the distribution of proteins needed for local changes in cellular dynamics. Outside the compartment, diffusion is the primary mode of soluble protein transport. Our findings suggest that cells possess previously unrecognized organizational strategies for managing soluble protein concentration and distributing them efficiently for activities such as protrusion and adhesion.</p>
},
	issn = {00063495},
	doi = {10.1016/j.bpj.2024.11.2032},
	url = {https://doi.org/10.1016/j.bpj.2024.11.2032},
	author = {Galbraith, Catherine G. and English, Brian P. and Boehm, Ulrike and Galbraith, James}
}
@article {69442,
	title = {Coumarin as a general switching auxiliary to prepare photochromic and spontaneously blinking fluorophores},
	journal = {bioRxiv},
	year = {2024},
	month = {2024 May 12},
	abstract = {<p>Single-molecule localization microscopy (SMLM) uses activatable or switchable fluorophores to create non-diffraction limited maps of molecular location in biological samples. Despite the utility of this imaging technique, the portfolio of appropriate labels for SMLM remains limited. Here, we describe a general strategy for the construction of {\textquotedblleft}glitter bomb{\textquotedblright} labels by simply combining rhodamine and coumarin dyes though an amide bond. Condensation of the ortho-carboxyl group on the pendant phenyl ring of rhodamine dyes with a 7-aminocoumarin yields photochromic or spontaneously blinking fluorophores depending on the parent rhodamine structure. We apply this strategy to prepare labels useful super-resolution experiments in fixed cells using different attachment techniques. This general glitter bomb strategy should lead to improved labels for SMLM, ultimately enabling the creation of detailed molecular maps in biological samples.</p>
},
	doi = {10.1101/2024.05.12.593749},
	url = {https://www.biorxiv.org/content/early/2024/05/12/2024.05.12.593749},
	author = {Jradi, Fadi M. and English, Brian P. and Brown, Timothy A. and Aaron, Jesse and Khuon, Satya and Galbraith, James A. and Galbraith, Catherine G. and Lavis, Luke D.}
}
