Welcome to Institute of Biochemistry II
Seminar in Biochemistry
6th Jan 2015
As reported in this month’s issue of Molecular Cell and Cell Host & Microbe, an international team of researchers led by Prof. Ivan Dikic has shed light on the molecular function of the protein PLEKHM1, that has previously been shown to regulate bone density in humans and rats. The team has identified two novel functions for the protein that are important for human disease; firstly, facilitating the removal of toxic protein aggregates and preventing their accumulation, which is relevant for diseases such as Parkinson’s. Secondly, controlling the intracellular growth of invading pathogens such as Salmonella. Both studies provide insight into the molecular mechanisms of cellular processes with high relevance to human diseases, and give rise to potential targets for therapeutic intervention.
2nd Jan 2015
Cells convert the energy extracted from foodstuff into ATP, the universal currency of cellular energy. Mitochondrial oxidative phosphorylation is carried out by five large enzyme complexes. The Zickermann group from Institute of Biochemistry 2 together with colleagues from the Cluster of Excellence Macromolecular Complexes in Frankfurt and from Freiburg University solved the 3D structure of mitochondrial complex I, the largest and most complex enzyme of this fundamental metabolic pathway. Complex I comprises more than 40 subunits and has a mass of almost 1 Mega-Dalton. Its major task is to pump protons across the inner mitochondrial membrane, thereby driving ATP synthesis. The exact mechanism, however, has remained elusive. In today?s issue of Science, the Zickermann group now reports new and exciting insights into the structure of this giant enzyme complex, explaining how it transmits the energy needed for proton pumping over quite a long range. The team was able to come up with a new model, by which a sequential formation of charged intermediates causes a concerted rearrangement of structural elements within the enzyme, thereby ultimately triggering proton translocation at the pump sites.
18th Dec 2014
EMBO will fund her work that is focused on understanding the role of linear ubiquitylation in tumor stromal crosstalk.
29th Sep 2014
25th Aug 2014
5th Aug 2014
21st Jul 2014
10th Jul 2014
|12th Jun 2014
SUMO-mediated control of a histone-modifying complex
The group of Stefan Müller unraveled a novel facet of SUMO-regulated gene expression. They discovered that the SUMO-specific isopeptidase SENP3 is needed for proper activity of histone-modifying MLL1/2 complexes. Removal of SUMO2/3 from the MLL1/2 subunit RbBP5 is required for the activation of a subset of HOX genes, including the regulator of osteogenic differentiation DLX3. The importance of this pathway for cell differentiation was demonstrated in a human stem cell model. The paper by Nayak et al. was published online in Molecular Cell on June, 12.
|25th Apr 2014
HFSP Program Grant for IBC2
The International Human Frontier Science Program (HFSP) Organization announced this year's winners of the competition for one of the prestigious HFSP research grants. Amongst the awardees is the Dikic group, who together with the Sidhu group (Canada), the Komatsu group (Japan) and the Sander group (U.S.) will receive 1,35 M USD for the next 3 years. "This award considerably pushes autophagy research in Frankfurt, especially because it funds one of our most innovative projects. Within the next 3 years, we expect to gain a lot of knowledge about molecular targeting of the autophagy network", says Ivan Dikic, IBCII director. Read more
|10th Apr 2014
The control of signaling in immunity and inflammation
The groups of Ivan Dikic and Masato Akutsu have moved closer in understanding how a novel form of protein modification, the linear ubiquitination, controls central pathways of immunity and inflammation. In a collaborative effort, they showed that the two enzymes responsible for assembling and disassembling linear ubiquitin chains are contained in one complex. By structural analysis, they managed to decipher the molecular details of the interaction between these two key enzymes and were able to show how the opposing activities of the complex are controlled. Their results are published in the current edition of Molecular Cell online.
|2nd Feb 2014
Deciphering the molecular mechanisms behind the cell's power packs
Complex I is the largest enzyme of the respiratory chain, a fundamental metabolic pathway operating to supply the cell with energy. Dysfunction of complex I causes numerous neuromuscular and neurodegenerative diseases in humans. Combining biochemical and structural evidence the Zickermann group now succeeded in shedding light on the essential role of accessory subunit NB4M (NDUFA6/LYRM6) for complex I function. The results are published in the current early edition of the journal PNAS (Angerer et al., doi: 10.1073/pnas.1322438111).
|24th Jan 2014
IBC2 and BMLS appointing two new group leaders
In a joint effort, IBC 2 and the Buchmann Institute (BMLS) recruited two new group leaders: Dr Anja Bremm (left) who received a prestigious Emmy Noether Fellowship from the German Research Foundation (DFG) and Dr Masato Akutsu (right) who will be heading a group endowed by the Leibniz Prize awarded to Ivan Dikic by the DFG. Both groups will be located in the BMLS on Riedberg campus, Anja Bremm mainly concentrating on cellular signaling, and Masato Akutsu strengthening the structural biology platform.
Link to BMLS Website
|22th Nov 2013
Structure of HOIP catalytic core solved
In collaboration with Katrin Rittinger at the MRC-NIMR in London, the Dikic group solved another molecular puzzle about the formation of specific Ubiquitin chains. In the current issue of Nature, they report the crystal structure of the catalytic core of HOIP, the critical enzymes involved in forming linear (Met1-linked) Ubiquitin chains. These chains are important regulators of cellular signalling, and knowing the molecular structure of the complexes involved is an important step forward to understanding how these pathways control innate immunity and inflammation.
Link to nature publication
|19th Nov 2013
Who's most cited of them all?
In its recent issue, Laborjournal (LJ) publishes a citation analysis in the field of cell biology covering the period from 2007 to 2010. Instead of asking the mirror, LJ searched the database "Web of Science" for authors based in Germany, Austria and Switzerland. Amongst the Top 5: IBC2 director Ivan Dikic with 1886 citations of 35 articles. One article from the Dikic lab made it under the Top 10 of most cited articles: the report about a role for the protein NBR1 in autophagy , published by Kirkin and collaborators 2009 in the journal Molecular Cell.
Link to article in Laborjournal
Link to Kirkin et al paper
|30th Oct 2013
Bless the team work
It took years to develop, and the input of scientists from five countries: BLESS, a novel technology for mapping DNA breaks by next generation sequencing. The resulting publication in Nature Methods by Crosetto, Dikic, Rowicka, and many colleagues is now featured by Laborjournal.
Link to LJ article in German
Link to original artcle
Link to BLESS website
|22th Oct 2013
LOEWE program Ub-Net recruitment drive
The LOEWE program Ubiquitin-Networks is a newly established interdisciplinary research network at the Goethe University which is led by Ivan Dikic.
The network recently received funding and is looking to recruit 1 Junior Group Leader, 1 Postdoc, and 12 PhD students. Deadline for applications is 7th November. Read full advertisement
|16th Oct 2013
New Group Leader
The IBCII welcomes Dr. Andreas Ernst from University of Toronto as independent group leader.
The research of his newly established protein engineering group is focussed on generating intracellular tools to study various signaling pathways.
Read more about Andreas Ernst
|25th Aug 2013
Award-winning cancer reseacher from Croatia
|8th Jan 2013
Professor Ivan Dikic receives Ernst Jung Prize for medicine
8th January 2013. The Jung Foundation for Science and Research announced that Frankfurt professor Ivan Dikic will receive the Ernst Jung Prize 2013 for his groundbreaking work in understanding the role of Ubiquitin in cellular signal regulation. The prize is awarded with 150,000 euro and will be presented at a ceremony on 3rd May in Hamburg.
Read more about Ivan Dikic
|6th Dec 2012
Leibniz Prize 2013 for Frankfurt professor Ivan Dikic.
In recognition of his groundbreaking work in decrypting the Ubiquitin code, Ivan Dikic is to receive the Gottfried Wilhelm Leibniz Prize 2013, Germany's most prestigious scientific award. The award is funded and presented by the German Research Foundation (DFG). It is the research prize with the highest endowment worldwide and comes with a grant of 2.5 M Euro.
Read more about Ivan Dikic
Ivan Dikic in DFG
|16th Oct 2012
Dr.Krishnaraj Rajalingam, an Emmy Noether Fellow from IBCII has been selected to be a PLUS3fellow of the Boehringer Ingelheim Foundation.
BIF will fund his research on Inhibitors of Apoptosis (IAPs) with a generous support of 825000 euros for the next three years.
|1st August 2012
2013 ASBMB William C. Rose Award goes to BMLS Director Ivan Dikic.
The Award honors the pioneering work of Ivan Dikic in understanding the Ubiquitin code, and his efforts in training and education of young scientists.
|18th June 2012
Seeing Ubiquitin chains in cells.
An international team of scientists led by IBCII director Ivan Dikic developed specific Ubiquitin biosensors for in vivo application. This approach might mark a major technical breakthrough in detection of Ubiquitin signals in living cells. It is published in today's online issue of Molecular Cell.
Link to full article
Read more about Molecular Signaling Group
|10th May 2012
A novel mechanism regulating SUMO-dependent protein networks.
The covalent attachment of the ubiquitin-like modifier SUMO to proteins serves an important mechanism for the control of protein-protein interactions. This is generally mediated via recognition of a SUMO-conjugate by an interaction partner that contains a specific SUMO interaction module, termed SIM (SUMO interaction motif). A major question is how the dynamics of SUMO/SIM interactions are regulated. Recent work done by Rebecca Ullmann in Stefan Muller's group together with co-workers from the Lombardi Cancer Center in Washington now uncovered an acetyl-dependent switch that determines the selectivity and dynamics of SUMO-SIM interactions (Molecular Cell, online May 10, 2012). In this context they show that acetylation of SUMO within a basic interface prevents binding to SIMs in PML, Daxx, and PIAS. One the other hand, acetyl-SUMO specifically binds to the Bromodomain of the co-activator p300. This acetyl-dependent switch of SUMO-mediated protein interactions attenuates SUMO-regulated gene silencing and affects the assembly of PML nuclear bodies. This work thus unravels a novel interplay of post-translational modifications that expands the regulatory repertoire of SUMO signaling.
Ullmann R, Chien C D, Avantaggiati M L, Muller S (2012) An acetylation switch regulates SUMO-dependent protein interaction networks, Mol Cell, online May 10, 2012, DOI 10.1016/j.molcel.2012.04.006
Read more about SUMO Signaling Group
|23th January 2012
Novel mechanism regulating cell shape and migration unveiled.
Cell shape and migration are controlled by RhoGTPases, a family of small GTPases whose activation is controlled by nucleotide binding. Rac1 is an important member of this family and
Read the full article
Read the HYS highlight
Read the research highlight from Nat. Rev. Mol. Cell Bio.
Read the faculty of 1000 evaluation
Read more about Krishna Rajalingam
|24th October 2011
Interview with Prof. Dr. Dr. Ivan Dikic, director of the Frankfurt Institute of Molecular Life Sciences (FMLS)
If you were granted one wish for the advancement of your research projects, what would this be?
Well, I've always valued and emphasized a creative atmosphere. It not only means being surrounded by intelligent people, but also having enough time
Read whole story here
Read more about Ivan Dikic
|13th September 2011
ERC Starting Grant awarded to Dr. Christian Behrends:
The ERC approved funding for his proposal on Xenophagy and bacterial avoidance (XABA). Briefly, microbial pathogens that successfully parasitize eukaryotic cells have evolved to evade autophagic microbial defenses (xenophagy) and subvert the host autophagic responses for their own survival and/or growth.
Whole story in Press release
More about Christian Behrends
|26th May 2011
New defense mechanism against Salmonella elucidated: infection with Salmonella, epithelial cells can get rid of the unwanted invader by a process called autophagy. In today's issue of the journal Science, an international group of scientists around IBC2 director Ivan Dikic describes how selectivity is achieved in this process.
Read full article or in Press release
|19th April 2011
A new Emmy Noether Fellow at the IBCII: Dr. Christian Behrends received the prestigious Emmy Noether Research Fellowship by the DFG. His independent group will be funded for three years with a perspective two3 years extension. The mammalian
More about Christian Behrends
|31st March 2011 - A step towards understanding chronic dermatitis: An international team of scientists led by IBCII director Ivan Dikic discovered a novel role for the protein SHARPIN in immune signalling.|
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| 1st Feb 2011 - IBCII is pleased to announce its new W2: Prof. Stefan Müller is appointed W2 professor in biochemistry at IBCII and will be an independant group leader for SUMO signaling group.
More about Stefan Müller
|1st Nov. 2010 - New group leader
Dr. Christian Behrends from Harvard Medical School in Boston will join IBCII as an independant group leader. He will establish the Autophagy signaling group.
More about Christian Behrends