Cell News Newsletter of the German Society for Cell Biology full electronic version Volume 41, 3/2015
DGZ International Meeting 2016 in Munich DGZ Awards 2016 The moment your data change scientifi c minds.
This is the moment we work for. Revolutionize Your Confocal Imaging
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www.zeiss.com/lsm CONTENT The moment your data change scientifi c minds.
This is the moment we work for. Revolutionize Your Confocal Imaging Newsletter of the German Society for Cell Biology
Executive Board Preface 4
President: Ralph Gräf (Potsdam) DGZ International Meeting – Munich-Martinsried, March 14 – 16, 2016 5
Vice President: Carien Niessen (Köln) DGZ Awards 2016
Chief Executive Officer (CEO): Walther Flemming Award 2016 6 Oliver Gruss (Heidelberg) Nikon Young Scientist Award of the DGZ 2016 7 Vice CEO: Klemens Rottner (Braunschweig) Binder Innovation Prize 2016 8
Advisory Board Werner Risau Prize 2016 9 M. Cristina Cardoso (Darmstadt) Thomas Dresselhaus (Regensburg) Reinhard Fässler (Martinsried) Research News Volker Gerke (Münster) // RECOGNITION Harald Herrmann-Lerdon Moritz Horn, Kira Allmeroth, Martin S. Denzel: MADE BY ZEISS (Heidelberg) “A sweet deal – modulation of amino sugar metabolism affects Ingrid Hoffmann (Heidelberg) protein quality and ageing” 10 Eugen Kerkhoff (Regensburg) Thomas Magin (Leipzig) Zeynep Ökten (München) Future Meeting 14 Britta Qualmann (Jena) Doris Wedlich (Karlsruhe) Impressum 16 Office: Sabine Reichel-Klingmann c/o Deutsches Krebsforschungs- Missing Members 16 zentrum (DKFZ) Im Neuenheimer Feld 280 69120 Heidelberg Tel.: 0 62 21/42-34 51 Cover image: The cover art shows a transgenic Caenorhabditis elegans roundworm. Fluorescent imaging Fax: 0 62 21/42-34 52 shows an animal that expresses a GFAT-1::CFP fusion protein under control of the GFAT-1 promoter. Discover the new ZEISS LSM 8 family of fast linear scanning confocals with GaAsP detection and GFAT-1 is the key enzyme of the metabolic hexosamine pathway and is most strongly expressed in the E-Mail: [email protected] animal’s pharynx and in the skin precursor cells, the so called seam cells. Airyscan. It offers high sensitivity, speed and 1.7× higher resolution in all three dimensions. Internet: www.zellbiologie.de (Martin S. Denzel, Max Planck Institute for Biology of Ageing, Cologne) Combine ZEISS LSM 800 and LSM 880 with Airyscan to perform quantitative imaging in life sciences.
www.zeiss.com/lsm Cell News 2/2015 3 PREFACE
Dear colleagues and friends,
we currently are in the midst of the arrangements for our next International Meeting, which will be held from March 14 – 16 in Munich. We are very happy that Prof. Heinrich Leonhardt from the LMU Munich agreed to join us as the local meeting president and to bring our International Meeting to one of the brightest hotspots for cell biological re- search in Europe. The venue will be at the biomedical center of the brand new university campus in Martinsried.
Meanwhile, we have some tradition in inviting societies from our neighboring countries to showcase their cell biological research. Like this year, when the Dutch Society for Cell Biology was our guest during the International Meeting in Cologne, we have invited the Austrian Association of Molecular Life Sciences and Biotechnology (ÖGMBT) to join next year’s meeting in Martinsried. Thus, Prof. Lukas Huber (University of Innsbruck) joined Heinrich Leonhardt and his organization team comprising Prof. Reinhard Fässler (MPI), PD Dr. Annette Müller-Taubenberger (LMU), and the DGZ executive committee. Moreover, we have implemented additional innovations: First of all, the Meeting will be shorter. Perso- nal communication with many members and our exhibitors, who are the most important sponsors of our meeting, suggested a more compact format. The Munich meeting will be held on three days with three plenary sessions and eight symposia covering the hottest topics in cell biology (see page 5 for the full list of topics). Moreover, sessions will be co- chaired by two scientists from Austria and Germany. In order to make the meeting more attractive to young scientists, symposia will have three slots for short talks selected from the abstracts instead of only two, and there will be an additional slot for very short flash talks, which may be used for “poster advertisements”. Thus, the stage is set for a lively and exciting meeting. Save the date, we would love to meet you there!
Cell biological research is an international issue. Thus, the executive committee has de- cided to follow the invitation to join the International Federation of Cell Biology (IFCB). The mission of the IFCB is to "promote international cooperation, and to contribute to the advancement of cell biology in all its branches" (wp.ifcbiol.org/). Membership is free of charge for our society. The IFCB organizes a very interesting meeting July 21 – 25 next year in Prague (www.iccb2016.org/), and has already announced a discount of 50€ for members of all IFCB societies including the DGZ.
Last but not least I would again like to encourage you to send articles for Cell News! Copyrights will remain completely yours and it is a wonderful chance to advertise your research to the cell biology community. To this end, you will find more information at zellbiologie.de/cellnews/for-authors/
Many regards,
Ralph Gräf (President)
4 Cell News 2/2015 INTERNATIONAL MEETING
DGZ International Meeting
Munich-Martinsried, March 14 – 16, 2016
Our meeting highlights the current state of research in the rapidly developing field of cell biology, a fundamental discipline for all life sciences. The format and programme of the meeting provides an international platform for presentation and discus- sion of the most recent and exciting achievements in cell bio- logy. We strongly support young scientists by short talks and poster sessions.
Our special guest for the International Meeting 2016 in Munich is the Austrian Association of Molecular Life Sciences and Bio- technology (ÖGMBT). Scientists working in Austria co-organize the scientific sessions and we especially encourage Austrian scientists to attend the meeting and to submit abstracts.
Photo David Kostner; file is licensed under the Creative The registration website will be announced on Facebook and Commons Attribution-Share Alike 2.0 Germany in the next issue of Cell News.
Meeting President: Legal Organizer (PCO): Exhibition & Sponsoring:
Prof. Dr. Heinrich Leonhardt MCI Deutschland GmbH MCI Deutschland GmbH LMU München Annika Bleckert Iohanna Vater Biozentrum Martinsried Markgrafenstr. 56 Markgrafenstr. 37 Dept. Bio II. 10117 Berlin, Germany 10117 Berlin, Germany Grosshaderner Str. 2 Phone: +49(0)30 / 204 59 27 Phone: +49 (0)30 / 204 59 37 D-82152 Martinsried Fax.: +49(0)30 / 204 59 50 Fax: +49 (0)30 / 20 45 9 - 50 Tel: 0049 (0)89 / 2180 - 74 232 E-mail: [email protected] E-mail: [email protected] Email: [email protected]
Topics and chairpersons
Plenary sessions: P1: Nuclear architecture/Gene regulation (Heinrich Leonhardt) P2: Cytoskeleton/Mechanosensing (Reinhard Fässler and Eugen Kerkhoff) P3: Membrane trafficking/sorting (Lukas Huber and Julia von Blume)
Symposia: S1: RNA biology/Non-coding RNAs (Michael Kiebler and Alexander Hüttenhofer) S2: Autophagy (Thomas Wollert and Claudine Kraft) S3: Visualization of membrane compartmentalization and dynamics (Thomas Ott and Petra Schwille) S4: Polarity and Signaling (Claus Schwechheimer and Elisabeth Knust) S5: Mitochondria (Barbara Conradt and Stefan Jakobs) S6: Migration/Adhesion (Barbara Walzog and Michael Sixt) S7: Cell cycle in cancer (Zuzana Storchova and Ludger Hengst) S8: Stem cells and Regeneration (Jan Lohmann and Maria Elena Torres-Padilla)
Cell News 2/2015 5 DGZ AWARDS 2016
WALTHER FLEMMING AWARD 2016
The German Society for Cell Biology offers a research award named after Walther Flemming, one of the pio- neers of cell biological research. In 1875 he provided us with a detailed description of processes during cell division, which he named mitosis. The Walther Flemming Prize is awarded annually for outstanding scientific merits from all fields of cell biological research. Eligible are researchers up to an age of 38 years. The award consists of a prize money of EUR 2000 and is sponsored by the European Journal of Cell Biology.
Applications have to consist of a cover letter, a CV and a list of publications. The subject of the application should relate to one distinct field of research. In addition, a short summary of the work and a compelling description of the importance of the work for cell biology should be presented.
Both individual applications and nominations are accepted. Applications will be reviewed by an independent commission of the DGZ. The award ceremony takes place at the next DGZ meeting, which will be held in March 2016 in Munich.
Please send your application by e-mail (and in parallel one hard copy by mail) to the DGZ office:[email protected]
Deutsche Gesellschaft für Zellbiologie e.V. (DGZ) Sekretariat, z.H. Frau Reichel-Klingmann c/o Deutsches Krebsforschungszentrum | Im Neuenheimer Feld 280 | D-69120 Heidelberg
Deadline for applications: January 15, 2016
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The German Society for Cell Biology (DGZ) and Nikon GmbH, auch mit Super Resolution Mikroskope offer a “Nikon Young Scientist Award of the German Society for Cell Biology“ for PhD students or young postdocs (within 3 years after graduating).
The award comprises a prize money of EUR 1500, sponsored by Nikon GmbH, Mikroskope.
Candidates are invited to apply for the prize by themselves or may be suggested by others. DGZ membership is required.
Applications have to consist of a cover letter, a CV and N-SIM PDF-files of publications that document the work of the applicant.
Applications will be reviewed by an independent commission of the DGZ. The award ceremony takes place at the next DGZ meeting, which will be held in March 2016 in Munich.
Please send your application by e-mail (and in parallel one N-STORM hard copy by mail) to the DGZ office:[email protected]
Deutsche Gesellschaft für Zellbiologie e.V. (DGZ) Sekretariat, z.H. Frau Reichel-Klingmann c/o Deutsches Krebsforschungszentrum Im Neuenheimer Feld 280 | D-69120 Heidelberg
Deadline for applications: January 15, 2016
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Nikon GmbH . Tiefenbroicher Weg 25 . 40472 Düsseldorf . Tel.: 0211 9414 888 . Fax: 0211 9414 322 . e-mail: [email protected] DGZ AWARDS 2016
BINDER INNOVATION PRIZE 2016
The BINDER Innovation Prize is founded by BINDER GmbH in Tuttlingen and awarded by the German Society for Cell Biology (DGZ). It is endowed with EUR 4000 and was awarded the first time in 1998. The award is given for outstanding cell biological research with a focus on cell culture or the use of cell cultures.
Candidates may apply for the prize themselves. DGZ membership is desired but not required.
Applications have to consist of a cover letter, CV and a research profile.
Applications will be reviewed by an independent commission of the DGZ. The award cere- mony takes place at the next DGZ meeting, which will be held in March 2016 in Munich.
Please send your application by e-mail (and in parallel one hard copy by mail) to the DGZ office: [email protected]
Deutsche Gesellschaft für Zellbiologie e.V. (DGZ) Sekretariat, z.H. Frau Reichel-Klingmann c/o Deutsches Krebsforschungszentrum | Im Neuenheimer Feld 280 | D-69120 Heidelberg
Deadline for applications: January 15, 2016
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WERNER RISAU PRIZE 2016 FOR OUTSTANDING STUDIES IN ENDOTHELIAL CELL BIOLOGY
The German Society for Cell Biology (DGZ) and the Werner-Risau-Prize committee will award a prize for "outstanding studies in endothelial cell biology" to candidates within the first five years after obtaining their PhD or MD (except in case of maternal leave). The prize will be awarded for an article already published or in press, and consists of a personal diploma and a financial contribution of EUR 4000.
For further details please visit: www.werner-risau-prize.org
Applicants are requested to send a letter of motivation together with their CV and one copy of the article by email (preferably in pdf format) to the
Werner Risau Prize Committee | c/o Prof. Dr. Rupert Hallmann Institute for Physiological Chemistry and Pathobiochemistry Westfaelische Wilhelms-Universitaet Muenster | Waldeyerstr. 15 | D-48149 Muenster, Germany E-mail: [email protected]
Deadline for applications: January 15, 2016
The prize will be awarded during the International Meeting of the German Society for Cell Biology (March 14-16, 2016) in Munich, Germany.
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“A sweet deal – modulation of amino sugar metabolism affects protein quality and ageing”
Moritz Horn1, Kira Allmeroth1,2, Martin S. Denzel1 1Max Planck Institute for Biology of Ageing | Joseph-Stelzmann-Str. 9b | D-50931 Cologne | Germany 2Cluster of Excellence in Cellular Stress Responses in Aging-associated Diseases (CECAD) Joseph-Stelzmann-Str. 26 | D-50931 Cologne | Germany contact: [email protected]
When organisms age, the fidelity of molecular maintenance lar signaling cascades that are induced particularly upon stress, mechanisms declines and cellular processes tightly controlled such as heat or oxidative environments, to maintain protein in young age go astray. A prime example is protein homeosta- integrity. These so-called unfolded protein response (UPR) net- sis, which includes the concerted interplay of protein synthesis, works are specialized to the respective subcellular compartment -modification, -folding, and -degradation. This tightly cont- (mitochondrial or endoplasmic reticulum (ER) UPR, and the cy- rolled network loses its equilibrium with age. To counter protein toplasmic heat shock response), but have in common that their homeostasis imbalances, organisms have evolved a set of cellu- induction triggers the expression of chaperones. Chaperones
ribosome folded protein vesicle 4 nascent N-glycan polypeptide endoplasmic 3 reticulum 1 2 folding cycle 5 misfolded proteasomal aggregation protein degradation chaperones UPRER ERAD autophagy
nucleus
Figure 1. ER Protein Homeostasis: Schematic representation of synthesis, folding, possible misfolding and degradation as well as transport of a secretory protein: Secretory proteins enter the ER lumen co-translationally (1) and become N-glycosylated (2) before entering the calnexin/calreticulin folding cycle (3). Proteins folded to their final conformation are shipped to the Golgi apparatus and the plasma membrane through vesicular transport (4). If chaperone- assisted protein folding fails (5), misfolded proteins trigger the endoplasmic reticulum’s unfolded protein response (UPRER), which in turn induces the expression of chaperones. Misfolded proteins can be shuttled to the cytoplasm via the ER-associated degradation (ERAD) machinery to become substrates for proteasomal or autophagic degradation. However, an overload of unfolded proteins can lead to toxic protein aggregation. GlcNAc Mannose Glucose
10 Cell News 2/2015 RESEARCH NEWS
in turn sequester unfolded proteins to support their folding. In lates HP activation and, as seen in GFAT-1 gof mutants, improves addition to chaperone assistance, successful protein folding protein quality control. Surprisingly, increased flux through the in the ER requires specific glycosylation of polypeptide chains, HP in GFAT-1 gof mutants does not induce canonical unfolded which, in addition to being structural components of the protein, protein response pathways, but activates protein degradative also reflect its folding state. In case all attempts to fold a nascent processes including ERAD, proteasome activity, and autophagy, protein in its natural conformation fail, unfolded proteins are all of which are required for the beneficial effects on an organism degraded by the proteasome or through the autophagic pathway. level. The proteome-protective effects of HP activation in the Naturally, the ER is particularly susceptible to proteotoxic stress nematode also require N-glycosylation and specific branches as it is a major site of protein synthesis and folding (Schröder of the UPRER, although both are not particularly elevated upon and Kaufman, 2005). The UPRER can be activated through three GFAT-1 activation. It can be speculated that increased UDP- distinct branches allowing cells a fine-tuned and highly specific GlcNAc levels in GFAT-1 gof mutants confer tunicamycin re- response to luminal protein folding imbalance. However, when sistance by directly competing with UDP-GlcNAc in glyco- the load of misfolded proteins increases they need to be retur- transfer reactions. However, it remains entirely elusive whether ned to the cytoplasm to become proteasome substrates. This the chaperone-independent improvement of proteome integri- clearance of malformed proteins from the ER is not a pas- ty is mediated through enhanced overall glycosylation, glyco- sive process, but uses the energy-dependent ER-associated sylation of specific regulatory proteins, or also involves degradation pathway (ERAD). In sum, organisms harbor a variety glycosylation-independent components such as direct alloste- of protein quality control mechanisms to maintain proteome ric functions of UDP-GlcNAc. Strikingly, increased HP flux does integrity that, however, lose capacity with age, thereby increasing not result in major changes of C. elegans transcriptional profile, the load of unfolded proteins and the susceptibility to proteo- indicating that posttranscriptional events underpin the induction toxic diseases, such as Alzheimer’s or Parkinson’s. Consistent- of protein quality control mechanisms found in C. elegans ly, improved protein homeostasis has been associated with GFAT-1 gof mutants. longevity in multiple species (Vilchez et al., 2014). In mammals, GFAT-1 is directly induced by one of the three Recent work identified the hexosamine biosynthesis pathway UPRER branches. In particular, studies in cardiomyocytes demons- (HP) as a key player in both protein quality control and trated that spliced X-box binding protein 1, a highly conserved longevity (Denzel et al., 2014). The first and rate-limiting enzyme signal transducer of the UPRER directly activates GFAT-1 expres- of the HP, glutamine-fructose-6-phosphate aminotransferase sion (Wang et al., 2014). Ischemia/reperfusion in the heart was (GFAT-1), shunts a fraction of fructose-6-phosphate from shown to trigger XBP-1 splicing and the subsequent HP activa- glycolysis into the synthesis of UDP-N-acetylglucosamine tion exerts robust cardioprotective effects. This protective stress (UDP-GlcNAc). This activated aminosugar serves as a substrate response is mediated via O-GlcNAcylation, which is in contrast for a variety of glycosylation reactions including ER-specific to findings inC. elegans, where key O-GlcNAcylating enzymes N-glycosylation, mucine-type O-glycosylation in the Golgi are dispensable for lifespan extension by GFAT-1 gof. These con- apparatus, and addition of single O-GlcNAc moieties to Ser/ tradictory findings might be explained by the limited knowledge Thr residues. All of these posttranslational modifications play a about C. elegans O-GlcNAcylation networks, which leaves the regulatory role in protein folding, Sekretion and function. opportunity that there is remaining enzymatic activity even after Moreover UDP-GlcNAc is a building block of highly abundant knockout of the key enzyme ogt-1. biopolymers such as chitin and glycosaminoglycans. The anabolic HP integrates various aspects of energy metabolism Across species, increased activity of the HP via GFAT-1 activation and is therefore under tight control: The key enzyme GFAT-1 is or GlcNAc supplementation results in downstream cytoprotec- negatively regulated by the HP’s end product UDP-GlcNAc (Assrir tive effects: In the nematode, this leads to enhanced systemic et al., 2014). In addition, the major energy-sensing AMP-activated fitness and longevity, while in mice it results in cardioprotection protein kinase (AMPK) as well as protein kinase A regulate through O-GlcNAcylation. Interestingly, supplementation with GFAT-1 activity through phosphorylation (Chang et al., 2000; the related amino sugar glucosamine (GlcN) results in lifespan Hu et al., 2004). extension in both worms and mice, however these effects are probably mediated via inhibition of glycolysis and subsequent Forward genetic screens in the nematode Caenorhabditis hormetic reactive oxygen species (ROS) signaling, independent elegans generated multiple GFAT-1 gain-of-function (gof) of the HP (Weimer et al., 2014). It is fascinating that small alleles that increase the flux through the HP leading to metabolites such as GlcNAc, GlcN, and a variety of others elevated levels of the product UDP-GlcNAc. Increased GFAT-1 including trehalose or α-ketoglutarate can slow the aging process activity not only overcomes toxicity caused by tunicamycin, a through distinct mechanisms (Chin et al., 2014; Honda et al., 2010). drug inducing protein misfolding stress in the ER by blocking Thereby the HP pathway in particular might work as energy N-glycan transfer, but also improves allover protein quality sensor linking the metabolic state to proteome integrity and control leading to longevity and protection from toxic protein survival. Despite this biological significance little is known about aggregation (Denzel et al., 2014). Importantly, supplementation the downstream mechanisms of increased HP flux. Thus, our with the HP precursor N-acetylglucosamine (GlcNAc) recapitu- lab is actively investigating the role of the HP in mammalian
Cell News 2/2015 11 RESEARCH NEWS
Glycolysis Glucose Glucose-6-P Fructose-6-P Pyruvate Gln UPRER Hexosamine pathway Glu GFAT-1 AMPK/PKA Glucosamine-6-P
N-acetylglucosamine (GlcNAc)
UDP-N-acetylglucosamine (UDP-GlcNAc)
biopolymers mucine-type N-glycosylation O-GlcNAcylation (chitin, GAGs) O-glycosylation
proteasome activity ERAD autophagy others?
protein homeostasis cardioprotection longevity
Figure 2: Hexosamine pathway flux affects protein homeostasis and longevity. The hexosamine biosynthetic pathway (HP) shunts a fraction of fructose-6-phosphate into the synthesis of the activated amino sugar UDP-N-acetylglucosamine (UDP-GlcNAc). UDP-GlcNAc serves as a building block for N- and O-Glycan structures, can be added to proteins as a single moiety, and is also a component of biopolymers such as chitin or glycosaminoglycans (GAGs). Activating the HP through gain-of-function mutation of the rate-limiting enzyme glutamine-fructose-6-phosphate aminotransferase (GFAT-1) or by supplementing N-acetylglucosamine (GlcNAc) induces protein quality control mechanisms (proteasome activity, ER-associated degradation (ERAD), and autophagy), resulting in increased lifespan and reduced proteotoxicity in the nematode C. elegans. In mammals, the ER unfolded protein response (UPRER) was shown to directly induce GFAT-1 expression, which exerts cardioprotective effects through increased O-GlcNAcylation. However, the mechanistic link between HP activation and improved protein quality control remains entirely elusive.
12 Cell News 2/2015 RESEARCH NEWS
protein quality control. Specifically, we are addressing the Biographies following questions: What are the major downstream effects of Moritz Horn studied bioche- GFAT-1 gain-of-function? What type of glycosylation and what mistry at the University of substrates are mostly affected by HP activation? Which particu- Tübingen, Germany. For his lar molecular changes trigger the proteome-protective effects? Ph.D. work he joined the lab of Altogether, this makes GFAT-1 an attractive target for research Adam Antebi at the Max Planck into the aging process including the prospect of using HP acti- Institute for Biology of Ageing, vation to counter proteotoxicity in human disease. Cologne, Germany, where he studied protein homeostasis in References the context of stem cell dyna- Assrir, N., Richez, C., Durand, P., Guittet, E., Badet, B., Lescop, E., and Badet-Denisot, M.-A. mics and development using (2014). Mapping the UDP-N-acetylglucosamine regulatory site of human glucosamine-6P synthase by saturation-transfer difference NMR and site-directed mutagenesis. Biochimie the nematode C. elegans. For 97, 39–48. his post-doc he stayed at the Chang, Q., Su, K., Baker, J.R., Yang, X., Paterson, A.J., and Kudlow, J.E. (2000). Phosphorylation Max Planck Institute and started in the new research group of of human glutamine:fructose-6-phosphate amidotransferase by cAMP-dependent protein kinase at serine 205 blocks the enzyme activity. J Biol Chem 275, 21981–21987. Martin Denzel to understand the role of hexosamine pathway Chin, R.M., Fu, X., Pai, M.Y., Vergnes, L., Hwang, H., Deng, G., Diep, S., Lomenick, B., Meli, V.S., flux in mammalian protein quality control and ageing. Monsalve, G.C., et al. (2014). The metabolite α-ketoglutarate extends lifespan by inhibiting ATP synthase and TOR. Nature 510, 397–401. Denzel, M.S., Storm, N.J., Gutschmidt, A., Baddi, R., Hinze, Y., Jarosch, E., Sommer, T., Hoppe, T., and Antebi, A. (2014). Hexosamine pathway metabolites enhance protein quality control Kira Allmeroth joined Martin and prolong life. Cell 156, 1167–1178. Denzel’s laboratory at the end Honda, Y., Tanaka, M., and Honda, S. (2010). Trehalose extends longevity in the nematode Caenorhabditis elegans. Aging Cell 9, 558–569. of 2014 to pursue her Ph.D. in Hu, Y., Riesland, L., Paterson, A.J., and Kudlow, J.E. (2004). Phosphorylation of mouse gluta- biological sciences. Before mo- mine-fructose-6-phosphate amidotransferase 2 (GFAT2) by cAMP-dependent protein kinase ving to Cologne, she did her increases the enzyme activity. J Biol Chem 279, 29988–29993. Schröder, M., and Kaufman, R.J. (2005). The mammalian unfolded protein response. Annu. Bachelors in biotechnology at Rev. Biochem. 74, 739–789. the University Bielefeld and Vilchez, D., Saez, I., and Dillin, A. (2014). The role of protein clearance mechanisms in orga- then studied molecular biome- nismal ageing and age-related diseases. Nat Commun 5, 5659. Wang, Z.V., Deng, Y., Gao, N., Pedrozo, Z., Li, D.L., Morales, C.R., Criollo, A., Luo, X., Tan, W., Ji- dicine at the Westfälische Wil- ang, N., et al. (2014). Spliced X-box binding protein 1 couples the unfolded protein response helms-University Münster for to hexosamine biosynthetic pathway. Cell 156, 1179–1192. her Masters. During that time, Weimer, S., Priebs, J., Kuhlow, D., Groth, M., Priebe, S., Mansfeld, J., Merry, T.L., Dubuis, S., Laube, B., Pfeiffer, A.F., et al. (2014). D-Glucosamine supplementation extends life span of she focused on the role of RNA- nematodes and of ageing mice. Nat Commun 5, 3563. binding proteins in ALS using the mouse as a model system.
Acknowledgements We would like to thank all members of the Denzel lab for support! This work is supported Martin Denzel studied Hu- by an ERC starting grant (640254 - MetAGEn), by a Marie Curie Career Integration Grant (CIG) (303714 - ER longevity), by a BMBF grant (EndoProtect), and by the Cologne Graduate man Biology in Marburg and School for Ageing Research. in Hamburg, Germany. He then went on to do his Ph.D. with Barbara Ranscht at the San- ford-Burnham Medical Re- search Institute in La Jolla, California, where he did cardio- vascular and tumor biology research. For his postdoc he joined Adam Antebi’s lab at the Max Planck Institute for Bio- logy of Ageing in Cologne, were he performed forward genetic screens for C. elegans mutants with improved protein quality control and extended lifespan. Since September 2014 he is an independent group leader at the Max Planck Institute Bio- logy of Ageing.
Cell News 2/2015 13 FUTURE MEETING
5th DSCB Trippenhuis Meeting “Building and repairing Tissues” Amsterdam, October 30, 2015
As board of the Dutch Society for Cell Biology DSCB we organize The Program the 5th DSCB Trippenhuis meeting entitled “Building and repairing Tissues”. 9:20 -9:30 Opening The meeting will take place on Friday, October 30, 2015 at “Het Trippenhuis” (KNAW building, Kloveniersburgwal 29). This location 9:30 - 10:10 is close to the Central Railway station in Amsterdam. (www.knaw. Clare Blackburn (Edinburgh, UK) nl/nl/de-knaw/het-trippenhuis) “Building and rebuilding the thymus”
For more information on the final program and registration see 10:10 - 10:45 attached files and our web site (www.cell-biology.nl). Niels Geijsen (Utrecht, The Netherlands) "iTOP, a novel tool for efficient modulation of primary cells" The Meeting is free of charge for members of the Dutch, Belgi- an and German Society for Cell Biology or participants that plan 10:45 - 11:15 Coffee to become member of the Dutch Society for Cell Biology (DSCB). Membership of the DSCB is 20,= Euro/year and payment starts in 11:15 - 11:55 2016. Paul Martin, (Bristol, UK), "Wound healing recapitulates embryo morphogenesis” Registration for non-members is 25,– Euro. Please transfer this amount to account number NL30 INGB 0000 4417 03 on the name 11:55 - 12:30 of "penningmeester Nederlandse Vereniging voor Celbiologie" (tre- Marie Jose Goumans (Leiden, The Netherlands) asurer of the Dutch Society for Cell Biology). Please mention in the “Cardiac progenitor cells to repair the injured heart”. payment name participant and registration costs TH meeting 2015. 12:30 - 13:05 Note Registration is required also for participants that don’t need Carlijn Voermans (Amsterdam, The Netherlands) to pay registration costs. “Advanced cellular therapies entering the clinic” Registration includes coffee/thee/lunch/and drinks after the mee- ting. 13:05 - 14:00 Lunch
Looking forward seeing you in Amsterdam. 14:00 - 14:40 Stefano Piccolo (Padova, Italy) The organizers, “YAP/TAZ in organ growth, tissue repair and cancer” Jaap van Buul, John Collard, Mar Fernandez-Borja, Peter Hordijk and Arnoud Sonnenberg 14:40 - 15:20 Anne Blangy (Montpellier, France,) "Targeting osteoclast adhesion to prevent bone resorption, a new weapon against osteoporosis?"
15:20 - 15:45 Coffee
15:45 - 16:20 Marcel Jonkman (Groningen,The Netherlands) “Revertant mosaicism: a healing source“
16:20 - 17:00 Hans Clevers (Utrecht, The Netherlands) “Lgr5 stem cells, organoids and human disease models”
17:00 Borrel
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Missing members: Impressum We have no valid address from the members listed below. If anybody can help us in this Publisher: respect, please send a message to the DGZ office at [email protected]. Deutsche Gesellschaft für Zellbiologie e.V. (DGZ) (German Society for Cell Biology) A Christine Hoffmann Stephan Peter Editor-in-Chief: Marwan Al Falah Jan Hönnemann Kirsten Peters Prof. Dr. Ralph Gräf (Universität Potsdam) Dorit Arlt J Alexander Petrovitch Editors: Thomas Jarchau Johannes Pohlner B Prof. Dr. Ludwig Eichinger Jennifer Baltes K R (Universität zu Köln) PD Dr. Oliver Gruss Tanja Barendziak Dieter Kaufmann Jürgen Rauterberg (Universität Heidelberg) Prof. Dr. Eugen Kerkhoff Friederike Bathe Tore Kempf Filomena Ricciardi (Universität Regensburg) Manuel Bauer Antje Kettelhake Astrid Riehl Prof. Dr. Friedemann Kiefer (MPI Molecular Biomedicine, Münster) Erich Knop Josef Rüschoff Wolfgang Bielke Prof. Dr. Thomas Magin Jessica Blume Karl-Hermann Korfsmeier S (Universität Leipzig) Prof. Dr. Carien Niessen Peter Brandt Martina Kralewski Gerd Schwarz (Universität zu Köln) Prof. Dr. Klemens Rottner Theo Brigge Bernd Krüger Sarah Schwarz G. Henriques (Techn. Universität Braunschweig) Andreas Brown Christian Kutzleb Every article stands in the responsibility of the author. Kyrill Schwarz-Herion For unsolicited sent manuscripts the society does not Julia Bubeck L undertake liability. Reproduction, also in part, only Udo Seedorf with permission of the society and with reference. C Stefan Lakämper Klaus Seidl Editorial Office Stacy Carl-McGrath Philipp Lange Manuscripts/Advertisements: Andrea Sokoll Sabine Reichel-Klingmann Rüdiger Cerff Friederike Lehmann Office of the German Society Karsten Spring D Lasse Lehnert for Cell Biology U c/o German Cancer Research Center Philip Dannhauser Joern Linkner Im Neuenheimer Feld 280 Nadime Ünver Susanne Dietrich M 69120 Heidelberg V Tel.: 06221/42-3451 Ulrich Drews Sabine März Fax: 06221/42-3452 Jürgen Voigt E-mail: [email protected] Anne Meinzinger F Internet: www.zellbiologie.de W Danai Feida Gottfried Mieskes Production: Wibke Wagner Michael Fredrich Elena Motrescu abcdruck GmbH Horst Waldvogel Waldhofer Str. 19 · 69123 Heidelberg Jürgen Frey Günter Müller [email protected] · www.abcdruck.de Diego J. Walther G Jens Müller Media Creation: Carolin Weise Anna Wagner · [email protected] Christiane Gerlach O Christiane Weydig Full electronic version H Adaling Ogilvie Stefan Winheim Frequency of publication: Kristina Hartmann P 4 issues yearly Detlev Herbst Andrea Pauli If you are interested in advertising, please contact the DGZ office Gerd Paulus Christoph Hinzen ([email protected])
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