The Berro lab develops experimental and quantitative methods for cell biology, biochemistry and biophysics to understand the molecular mechanisms of fundamental cellular processes. Our research is currently focused on unraveling how the molecular machinery of clathrin-mediated endocytosis generates forces to deform the plasma membrane and conversely how this machinery senses membrane tension and adapts to it.
Check out our new review on the molecular mechanisms of force production in clathrin‐mediated endocytosis! https://t.co/ADGKxo8jK4 pic.twitter.com/on8pRROkhv
— Berro Lab ???? (@BerroLab) July 16, 2018
Our book on quantitative methods to study endocytosis is out! https://t.co/M0czqm0i2v@MorganClaypool @WallaceUcsf pic.twitter.com/f0uxiReeng
— Berro Lab ???? (@BerroLab) August 15, 2018
New modeling preprint based on some of the very first experiments I ever did in @Lblanchoin lab! https://t.co/fz3SpEulUR
— Berro Lab ???? (@BerroLab) June 13, 2018
— Berro Lab ???? (@BerroLab) June 13, 2018
The Berro lab has a new doctor in the house. Congrats Mike Lacy! pic.twitter.com/iofCIf0Xx8
— Berro Lab ???? (@BerroLab) May 22, 2018
Our paper on the conversion of binding energy into elastic energy via actin filament crosslinking is now published in @PLOSCompBiol: Structural organization and energy storage in crosslinked actin assemblies https://t.co/3SGktFCeB4
— Berro Lab ???? (@BerroLab) May 31, 2018
This coffee-stirrer-and-spring model summarizes it all! pic.twitter.com/JHR2YBNMMN
— Berro Lab ???? (@BerroLab) May 31, 2018
Our simulations uncovered new mechanisms for the conversion of binding energy into elastic energy, and subsequently into torque, via dynamic actin filament crosslinking.
https://www.biorxiv.org/content/early/2017/12/20/237412
Mike’s single molecule study of the eisosome has been published in MBoC.
http://www.molbiolcell.org/content/28/17/2251.full
A few plasmids that were created in the Berro lab and can be useful for the S. pombe community are now available on Addgene. These include plasmids to perform CRISPR/Cas9 edition using fluoride selection (Fernandez and Berro, 2016), and plasmids to C-terminally tag proteins with SNAP, CLIP, Halo, mEOS3.2, PAmKate, PATagRFP or PAmCherry (unpublished).
New single-molecule imaging of the eisosome BAR domain protein Pil1p reveals filament-like dynamics.
bioRxiv
BIORXIV/2016/092536
Abstract
Molecular assemblies can have highly heterogeneous dynamics within the cell, but the limitations of conventional fluorescence microscopy can mask nanometer-scale features. We have developed a novel, broadly applicable, fluorescent labeling and imaging protocol, called Single-molecule Recovery After Photobleaching (SRAP), which allowed us to reveal the heterogeneous dynamics of the eisosome, a multi-protein structure on the cytoplasmic face of the plasma membrane in fungi. By fluorescently labeling only a small fraction of cellular Pil1p, the core eisosome BAR domain protein in fission yeast, we visualized whole eisosomes and, after photobleaching, recorded the binding of individual Pil1p molecules with ~20 nm precision. Further analysis of these dynamic structures and comparison to computer simulations allowed us to show that Pil1p exchange is spatially heterogeneous, supporting a new model of the eisosome as a dynamic filament.