Our kinetochore paper is selected for the 65th birthday collection of JCB

For the collection celebrating the 65th anniversary of the Journal of Cell biology, our paper Functional Analysis of Kinetochore Assembly in Caenorhabditis elegans was selected for its contribution to “dissecting the mechanics of cell division”. The paper from 2001 by Karen and Arshad, postdocs in our lab at the time has great company there. Click here for the link


GFP-histone H2B was used to visualize chromosome segregation during the first mitotic cell division

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Tony wins 2020 Wiley Prize in Biomolecular Sciences

Tony wins the 19th annual prize together with Clifford Brangwynne of Princeton university and Michael Rosen of the Southwestern University in Texas for their work on defining phase-separated biomolecular condensates. In a statement of the Wiley foundation their work was recognized for…

revealing a new principle for subcellular compartmentalization based on formation of phase-separated biomolecular condensates, a process implicated in both physiological and pathological events

Since 2002 the prize has recognized “breakthrough research in pure and applied life sciences research”. Past prize winners “have been chosen because of their breakthrough research in areas as diverse as genetics, cell motility, folded proteins and siRNA. The impressive list of past recipients includes winners of the Nobel Prize and the Lasker Prize in basic medical research”

Congratulations to Tony, Cliff and Mike and all their coworkers in their labs!

click here for the original press announcement.

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Enrichment of soluble tubulin at centrosomes

Recent work from Dresden (2017) suggests that centrosomes are condensates that nucleate in part by concentrating soluble tubulin. Here we show that indeed tubulin is extremely concentrated at centrosome in C. elegans embryos, suggesting that such a tubulin concentration could indeed play a key role in nucleation.

References

1-https://www.ncbi.nlm.nih.gov/pubmed/28575670

2-https://www.ncbi.nlm.nih.gov/pubmed/31636117

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Tony wins Carl Zeiss lecture award

The award to Tony comes from the German Society for Cell Biology for excellent achievements in research and was established in 1990 by the company Zeiss. Tony will lecture on September 27th in Tübingen during the fall conference of the German Society for Biochemistry and Molecular Biology (GBM) and the German Society for Cell Biology (DGZ). read more: Press release from the MPI-CBG and press release from Zeiss

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Small molecules that dissolve stress granules

In ALS, a mutated nuclear protein, FUS (fused in sarcoma), mislocalises to the cytoplasm and aggregates in stress granules. This leads to a liquid to solid transition of the granules and a consequent degeneration of the motor neuron (motor neuron die-back ). We show that lipoamide and lipoic acid can prevent the aggregation of FUS and consequently the die-back of patient-derived motor neurons in cell culture. It also reduced protein aggregation in C. elegans and induced the recovery of motor defects in transgenic D. melanogaster expressing a mutant FUS.

This study takes advantage of the recent advances in understanding liquid-liquid phase separation in health and disease. Read more.

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Suzanne Eaton

We, past and current members of the Hyman lab, are reeling from the sudden and tragic loss of Suzanne Eaton. She was a wonderful person who lives on in our hearts. In this difficult time, we stand together with her family and colleagues.

https://www.mpi-cbg.de/suzanne-eaton/

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FlexiBAC, our open source protein expression system

One of great things here at the MPI-CBG are our Service and Facilities, among them the protein expression facility (PEPC), which has been heavily used by us in recent years. In collaboration with Jeff Woodruff, a former postdoc, they developed FlexiBAC, an amazingly versatile protein expression system in insect cells, which was developed with a huge range of different constructs and tags, which might fit your needs as well.

Have a look at the original publication here .Plasmids are available at Addgene.

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We held the first EMBO phase separation course here at the MPI-CBG

From 4th to 13th February we taught our first EMBO course

Methods for Studying Phase Separation in Biology here in Dresden at the MPI-CBG and CSBD.

The course was organized together with the Tang and Alberti lab, including morning lectures, theoretical or experimental parts during the day and a relaxing evening part. Importantly, we included as well the project ideas of our participants. They came from 12 different nations in Europe, Asia and America and made the course truly international and fun!



tweezer fun
condensates in cells

evening relaxation


Surprise from our participants!


We are still amazed by the great feed back we got, it was a big success for all of us, and most importantly for our participants!

Check out @Hymanlab and #EMBOPhaseSeparation on Twitter for more


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Phase separation buffers noise in cells



Now, the paper got published in Science! Congratulations to Adam and all the coauthors. And check out the perspective article about the paper from the Brangwynne lab (@Brangwynnelab), as well as the press article from the CSBD and from the CBG .

We are excited to share our pre-print which explores how phase separation affects noise in cells. The question of how cells manage to tightly control protein concentrations has been a long-standing challenge in biology. In collaboration with the Zechner and Jülicher groups, we now show in theory and experiments that liquid-liquid phase separation (LLPS) can be a very effective mechanism to buffer protein concentrations against gene expression noise.



The protein condensates used in our study dissolve during mitosis so that the protein concentration in the dilute, bulk phase is no longer buffered and variability becomes apparent.

In conclusion our results suggest a novel role of phase separation for gene regulation and biological information processing.


See below a mitosis movie of the tagged DDX4 protein construct


Click for the pdf of the preprint or go to the biorxiv page

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Rheology of protein condensates using optical traps

An increasing number of proteins with intrinsically disordered domains have been shown to phase separate in buffer to form liquidlike phases. These protein condensates serve as simple models for the investigation of the more complex membraneless organelles in cells. To understand the function of such proteins in cells, the material properties of the condensates they form are important.


Fig: scheme of the set up based on a dual optical trap

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Louise and her coworkers now developed a novel method based on optical traps to study the frequency-dependent rheology and the surface tension of P-granule protein PGL-3 condensates as a function of salt concentration. Have a look at the pdf or follow the link below.

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