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ATP as a biological hydrotrope — congratulations to Avinash, Liliana, and colleagues on their paper in Science, in collaboration with Yamuna Krishnan from UChicago!

Our latest publication, in collaboration with Yamuna Krishnan in Chicago, is out today in Science! In this work, we show that ATP can act as a biological hydrotrope, keeping proteins soluble. Hydrotropes are amphiphilic small molecules that solubilize hydrophobic molecules in aqueous solutions. While ATP is most commonly known as the energy source for cells, there is ~100 times more ATP in the cell than it needs for energy-related purposes. We show that at this high physiological concentration, ATP can act as a hydrotrope, both preventing the formation of and dissolving previously formed protein aggregates. This has interesting implications for aggregation associated with age-related neurodegenerative diseases, as the levels of ATP in cells decline with age. Read the full paper in Science (free full text/PDF links here) and watch our video abstract below or on sciencesketches.org! You can also read a perspective on our paper by Allyson Rice and Mike Rosen in the same issue of Science. 

 

 

ATP as a biological hydrotrope 
Avinash Patel*, Liliana Malinovska*, Shambaditya Saha, Jie Wang, Simon Alberti, Yamuna Krishnan#, Anthony A Hyman#
Science. 2017 May 18;356(6339):753-756. (links to free Full Text & PDF versions can be found on our Publications Page)

* first authors
# corresponding authors

Read our reviews to learn about “Liquid-liquid phase separation in biology”, “Are aberrant phase transitions a driver of cellular aging?”, and “Biomolecular condensates: organizers of cellular biochemistry”

Everything you ever wanted to know about our current understanding of cytoplasmic organization by phase separation, from the physics behind it to the consequences for disease, in one comprehensive review:

Liquid-liquid phase separation in biology.
Hyman AA, Weber CA, Jülicher F.
Annu Rev Cell Dev Biol. 2014 Oct 11;30:39-58.

2016 UPDATE: Also read a new review and perspective by Tony Hyman and Simon Alberti in Bioessays:

Are aberrant phase transitions a driver of cellular aging?
Alberti S, Hyman AA.
Bioessays. 2016 Oct;38(10):959-68. doi: 10.1002/bies.201600042. Epub 2016 Aug 24.

2017 UPDATE: New review in Nature Reviews Molecular Cell Biology!

Biomolecular condensates: organizers of cellular biochemistry. [PDF]
Banani SF, Lee HO, Hyman AA, Rosen MK.
Nat Rev Mol Cell Biol. 2017 Feb 22.

Impact of water in a water-surface

Image credit: Marlon Felippe, Wikimedia Commons

An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function

New work from the Hyman and Alberti labs uncovers an important role for chaperone proteins in preventing aberrant phase transitions in stress granules. See a brief synopsis below and read the full paper online. Congratulations to all of the authors on this work!

Synopsis

The presence of misfolded protein in stress granules alters their dynamic state and induces a phase transition. This process is counteracted by chaperones and autophagy, acting as a stress granule quality control system.

  • Misfolded proteins have a tendency to aggregate in stress granules (SGs).

  • Misfolded proteins promote a conversion of SGs into an aberrant solid‐like state.

  • Chaperones prevent the formation of aberrant SGs and promote SG disassembly.

  • Persistent aberrant SGs are targeted to the aggresome for degradation.

An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function.
Mateju D, Franzmann TM, Patel A, Kopach A, Boczeck EE, Maharana S, Lee HO, Carra S, Hyman AA, Alberti S.
The EMBO Journal. (2017) e201695957. [FullText]

Kate Lee selected as L’Oréal-UNESCO For Women in Science International Rising Talent

Congratulations to our phenomenal postdoc, Kate Lee, on this prestigious honor!

“Kate Lee, postdoc at the MPI-CBG Hyman Lab, is the first scientist living and working in Germany to be selected as “International Rising Talent”. The L’Oréal-UNESCO For Women in Science International Rising Talents are presented to fifteen promising young women, from each world region (Africa and the Arab States, Asia-Pacific, Europe, Latin America and North America), in order to support and encourage them to pursue their scientific careers.

Kate Lee works on understanding how proteins turn into pathological aggregates in neurodegenerative diseases upon aging. Her findings can contribute to a better understanding of diseases like Parkinson’s and become the foundation of potential new therapies.

The L’Oréal-UNESCO For Women in Science initiative began 19 years ago. Since that inaugural year, the L’Oréal Foundation and UNESCO have strived to support and recognize accomplished women researchers, to encourage more young women to enter the profession and to assist them once their careers are in progress. Much remains to be done with regard to gender balance in science. Most tellingly, women account for only 28% of the world’s researchers according to the UNESCO Science Report 2015. There are still great barriers that discourage women from entering the profession and obstacles continue to block progress for those already in the field.”

– MPI-CBG Press Release

Advice for young group leaders

Yesterday, Tony gave the EMBO Keynote Lecture at the Young Investigators’ Meeting in Goa, India. In his lecture, titled “From zoology to physics — how to avoid staying in your comfort zone,” Tony gave advice on how to be a successful young group leader.

Below, you can watch another talk he gave on a similar topic at the MPI-CBG in 2014. Tony spoke as part of a summer seminar series hosted by MPI-CBG postdocs during which group leaders gave thoughtful and personal advice about how to start your own group. Tony focused on the main goal of starting your own group — to discover something important — and how to stay on track towards achieving that goal.

New Review: “Biomolecular condensates: organizers of cellular biochemistry”

Congratulations to our postdoc Kate Lee, Tony, and co-authors Salman Banani and Mike Rosen of UTSW on their new review, “Biomolecular condensates: organizers of cellular biochemistry.” Read the full article using the links below.

Biomolecular condensates: organizers of cellular biochemistry. [PDF]
Banani SF, Lee HO, Hyman AA, Rosen MK.
Nat Rev Mol Cell Biol. 2017 Feb 22.

Biomolecular condensates are micron-scale compartments in eukaryotic cells that lack surrounding membranes but function to concentrate proteins and nucleic acids. These condensates are involved in diverse processes, including RNA metabolism, ribosome biogenesis, the DNA damage response and signal transduction. Recent studies have shown that liquid–liquid phase separation driven by multivalent macromolecular interactions is an important organizing principle for biomolecular condensates. With this physical framework, it is now possible to explain how the assembly, composition, physical properties and biochemical and cellular functions of these important structures are regulated.

The Benefits of a “Central Service” for Biology Preprints

Visit the ASAPbio website to learn about a new proposal to create a Central Service for biology preprints. The relationship of this Central Service to existing preprint servers would be akin to the relationship between PubMed and scientific journals. ASAPbio has released a Request for Applications (RFA) for the development of a Central Service for biology preprints, proposals for which are due on April 30, 2017.

How did life begin? Dividing droplets could hold the answer. (Article in Quanta Magazine)

The story of our publication in Nature Physics, “Growth and division of active droplets provides a model for protocells,” has been picked up by Quanta Magazine (and re-published in Wired Magazine as well).

Read the full story here! 

Lucy Reading-Ikkanda/Quanta Magazine

Cover of Trends in Molecular Medicine

Belated congratulations are in order to the authors and illustrators of the cover article for the September issue of Trends in Molecular Medicine! See the cover and associated description below.

Common molecular pathways in Amyotrophic Lateral Sclerosis and Frontotemporal Dementia. Jochen H. Weishaupt, Tony Hyman, Ivan Dikic. Trends in Molecular Medicine, 2016. [PDF][PubMed]

Web

“Amyotrophic lateral sclerosis and frontotemporal dementia are related dementias. On pages 769–783, Dikic and colleagues discuss recent findings associating autophagy, vesicle trafficking, and RNA metabolism to neuronal death, identifying common links between these dementias. The cover evokes the therapeutic potential of manipulating such cellular processes to “eat away” at pathogenicity in the brain. Yellow ‘Pacmen’ symbolize ‘autophagy’. Yellow dots represent ‘physiological stress granules’, maturing into ‘bad stress granule monsters’ (light blue, center). The monsters symbolize ‘mitochondria’, ‘protein aggregates’ and ‘aberrant stress granules’. Illustration by Julia Eichhorn. Cover design by Catarina Sacristán.”

New publication: Growth and division of active droplets provides a model for protocells

The latest work in our ongoing collaboration with the lab of Frank Jülicher is now out in Nature Physics. Congratulations to all the authors!

Growth and division of active droplets provides a model for protocells
David Zwicker, Rabea Seyboldt, Christoph A. Weber, Anthony A. Hyman & Frank Jülicher, Nature Physics (2016)

Abstract
It has been proposed that during the early steps in the origin of life, small droplets could have formed via the segregation of molecules from complex mixtures by phase separation. These droplets could have provided chemical reaction centres. However, whether these droplets could divide and propagate is unclear. Here we examine the behaviour of droplets in systems that are maintained away from thermodynamic equilibrium by an external supply of energy. In these systems, droplets grow by the addition of droplet material generated by chemical reactions. Surprisingly, we find that chemically driven droplet growth can lead to shape instabilities that trigger the division of droplets into two smaller daughters. Therefore, chemically active droplets can exhibit cycles of growth and division that resemble the proliferation of living cells. Dividing active droplets could serve as a model for prebiotic protocells, where chemical reactions in the droplet play the role of a prebiotic metabolism.

New preprint: The centrosome is a selective phase that nucleates microtubules by concentrating tubulin

The Hyman lab is proud to publish preprints, which we post in parallel to journal submission. You can find our latest manuscript on bioRxiv, and we welcome your feedback:

The centrosome is a selective phase that nucleates microtubules by concentrating tubulin
Jeffrey B Woodruff, Beatriz Ferreira Gomes, Per O Widlund, Julia Mahamid, and Anthony A Hyman

Photo from lab dinner at ASCB

Here’s a quick photo from last week’s Hyman lab dinner during ASCB 2016 in San Francisco! It was great to see former members like Laurence Pelletier and Garrett Greenan, as well as collaborators Elvan Boke and Marco Hein.

See you next year at the joint ASCB/EMBO meeting in Philadelphia!

Current and former Hyman lab members out to dinner during ASCB 2016

Current and former Hyman lab members out to dinner during ASCB 2016

Annual Christmas Market outing

After Tony’s annual vision talk at our “Lab Day,” everyone gathered for glühwein and cheer at our traditional trip to the Neumarkt Christmas Market. Happy holidays, everyone!

xmasmarket2016

The most colorful safety briefing

Our brilliant baker and Masters student Stephen helped make the annual safety briefing much more festive this year. Check out his incredible rainbow cake! cake4 cake5 cake6 cake2 cake1 cake3

New! Video abstract for “Amyloid-like self-assembly of a cellular compartment”

Watch the video abstract for Boke et al 2016, “Amyloid-like self-assembly of a cellular compartment,” and see the full post about it on the Science Sketches website!

Come see us at ASCB 2016!

The Hyman lab is represented at the 2016 ASCB annual meeting, taking place now in San Francisco. Come see us if you’re here!

• Sunday, Dec 4, 12pm-1:30pm: Louise Jawerth presents her poster, “The liquid to gel transition in protein droplets” (poster B1345)

• Sunday, Dec 4, 5:20pm-5:35pm: Shamba Saha gives a talk, “An mRNA competition mechanism regulated localized phase separation of liquid-like P granules in C. elegans embryo,” Room 103

• Monday, Dec 5, 12:28-12:35pm: Elvan Boke gives a talk, “Amyloid-like self-assembly of a cellular compartment,” Microsymposia Room 2 Hall C

• Monday, Dec 5,1:30pm-3:00pm: Jeff Woodruff presents his poster, “The centrosome is a selective phase that nucleates microtubules by concentrating tubulin” (poster B342)

Yesterday (Dec 3), Tony spoke at the ASAPbio session to advocate for the use of pre-prints in Biology, and he also spoke at the stem cell session, giving a talk entitled, “Cell biology of the stem cell to neuron transformation.”

Finally, Lisa Dennison will be at all 3 Science Discussion Tables (Dec 4, 11am-12pm; Dec 5, 3-4pm; Dec 6, 11am-12pm), discussing sciencesketches.org

We hope to see you here in San Francisco!

On Research Funding and the Power of Youth

Read the full essay on the importance of funding young scientists, written for the President’s Column of the October issue of the ASCB newsletter by Tony Hyman, Ashad Desai, and Peter Walter.

“On Research Funding and the Power of Youth” – PDF

Video: Interview with Tony about phase transitions and disease

Watch a video of Tony explaining phase transitions and disease on the new website “Latest Thinking,” which is a video collection of researchers explaining their latest breakthroughs. Be sure to also check out the videos of Tony answering other short questions in the “Beyond” section just below the main video.

Congratulations to Oliver, Jeff, and colleagues on their paper & video abstract in Biology Open, investigating regulation of centrosome assembly

In new work published this month in Biology Open, Oliver Wueseke, David Zwicker, Jeff Woodruff, and colleagues show that PKL-1 phosphorylation of the centrosome scaffold protein SPD-5 is a key regulatory step which determines centrosome size and density. Importantly, they show that this step is not necessary for proper maintenance or function of the centrosome. Watch their Science Sketches video abstract below, and read the full article online, which is currently featured on the Biology Open home page!

Polo-like kinase phosphorylation determines Caenorhabditiselegans centrosome size and density by biasing SPD-5 toward an assembly-competent conformation
Oliver Wueseke*, David Zwicker*, Anne Schwager, Yao Liang Wong, Karen Oegema, Frank Jülicher, Anthony A. Hyman, Jeffrey B. Woodruff
Biology Open 2016 5: 1431-1440; doi: 10.1242/bio.020990

Welcome, Ceciel, our newest PhD student!

The Hyman Lab welcomes Ceciel Jegers, our newest PhD student. Ceciel comes to us from the Netherlands, and she will be working on phase transitions in cells and disease.
jegers_ceciel

  • Archives


  • Selected Essays

















  • Recent Videos


    An interview with Tony about Phase Transitions and Disease


    Phase separation in cell polarity: Saha et al, Cell 2016


    Encouraging Innovation, iBiology.org


    The genetics linking temperature and fertility in worms: Leaver et al, Biology Open 2016


    Cell PaperFlick on Phase Transitions in Disease


    Check out this playlist to watch all the videos in our "Two Minute Talk" Series


    Ways of Growing, a film created for the MitoSys Project


    What is a Discovery?


    Embryonic Development of C.elegans