Plants cannot run away! Instead, over millions of years of evolution, they have developed smart strategies to quickly respond and deal with the sudden changes in their environment. Such changes are experienced as stress, which can be of biotic- (e.g. pathogens, herbivores) or abiotic nature (e.g. cold, heat, salinity, drought). Our main focus is to understand the molecular mechanism by which plant cells sense these stress signals, how these signals are intracellularly transduced, and how they are eventually converted into appropriate cellular responses that allow the plant to deal with the stress. We are specifically interested in the signal transduction of temperature stress (cold, heat), water stress (drought, salinity and hypoosmotic stress), and during plant-microbe interactions.
Research in the lab of Plant Cell Biology is focussed on the role of phospholipids in Stress Signalling & Development. Especially, lipid second messengers phosphatidic acid (PA), DGPP and polyphosphoinositides, like PIP and PIP2, have our interest. These molecules are present at very low concentrations in cellular membranes and are rountinely missed by common lipidomic analyses. Nonetheless, these minor signalling lipids can easily be picked up by 32Pi-labelling (see TECHNIQUES) because their turnover is much faster than structural phospholipids and because they are synthesised via lipid kinases that use ATP, which is one of the first compounds labelled. Key players involved in PA and PPI metabolism are depicted in the scheme above. Routinely, this involves PLC-and PLD signalling cascades and a variety of lipid and inositolphosphate kinases. Note that PA can be generated through both PLC- and PLD pathways, which likely occurs at different cellular- and subcellular locations and in response to different stimuli, and resulting in different outputs.
Phospholipids are routinely analysed using in vivo 32P-orthophosphate (32Pi)-labelling. In general, cells-, seedlings- or tissues like leaf discs are used, and labelling times vary from min to hrs or O/N, depending on the type of experiment (e.g. turnover vs mass levels). To monitor PLD activity in vivo, transphosphatidylation assays are conducted, which use primary alcohols as substrate (see 'All Publications' ref 9, 18). Shown is an example of the green alga Chlamydomonas. Cells were prelabelled for 4 hrs and then stimulated for 5 min in the presence and absence of a low concentration of a primary alcohol that cells don't mind. Lipids were then extracted and chromatographed using an Ethylacetate TLC system that separates phosphatidylalcohols from other phospholipids (panel a). PLD catalyses the transphosphatidylation so the production of 32P-labelled phosphatidylalcohols is a relative measure for in vivo PLD activity. Autoradiography visualises their positions while PhosphoImaging is used for their quantification. We have found that PLD is activated in response to various environmental stresses, including, heat, drought, salt, and in response to pathogens. Arabidopsis contains 12 PLDs, rice 17. We are still investigating which PLD does what.
Using time-course experiments, the timing and duration of PLD activation can be established. Similarly, the activation of PLC, and PI-, PIP-, DAG- and PA kinase can be analysed. For this, lipids are chromatographed by an Alkaline TLC system (panel b). Note the hydrolysis of PIP2 (PtdInsP2) within 15 sec to produce DAG that is converted to PA by DAG kinase. PI- and PIP-kinase activities also increase to maintain PIP2 levels. Since PLC is down regulated before these lipid kinases are, PIP and PIP2 are transiently over-produced. In the same time frame, the PA signal is attenuated by PA kinase producing DGPP. Figure is adapted from Ref. 27. Note that 'flowering plants' contain 30- 100- fold lower levels of PIP2 than Chlamydomonas or animal cells. This discrepancy has major consequences for the interpretation of lipid signalling in plants and what PLC takes as substrate in vivo (see ref. 70).
Since both PLD and DGK can generate PA as second messenger, it is crucial to be able to ditinguish between both pathways. Moreover, PA can also be intermediate in the synthesis of structural phospholipids via acylation of lyso-PA. To distinguish between these PA pools, we have setup a Differential Labellling protocol. It uses the fact that for PA to become radioactive, one only needs relative short labelling incubation times for the DGK and long for the PLD. This is because DGK requires ATP to make PA and this is one of the first components to become labelled when cells are incubatred with 32Pi, while PLD requires a 32P-labelled structural lipid like PE to generate 32P-PA and this takes hours of metabolic labelling (see top panels). Moreover, using the transphosphatidylation assay, one can check after how long labelling, the structural lipid pool is able to generate a radioactive PA and PBut.
In the pannels below show the practice for Chlamydomonas cells that were metabolically labelled with 32Pi for the times indicated, and were subsequently treated for 1 min with buffere alone (control; panel A, B) or with a stimulus (in this case 1 µM mastoparan in buffer (panel C, D), both in the presence of 0.1 % n-butanol. Lipids were then extracted, split into half, and either seperated on EtAc TLC (A, C) to separate the PLD-catalyzed phosphatidylbutanol (PBut), or Alkaline TLC (B, D) to visualize the rest of the phospholipids, including PA and its phosphorylated product, DGPP. The point is that all cells were treated for the same time period (1 min) but that the PBut only became radioactive when its substrate (i.e. PE) started to be labelled (>40min). The same would hold for the PA that would be generated through PLD. In contrast, when PA was generated via DGK, then the label would come from ATP, and since this compound is labelled within sec, an increased radioactive PA response could be witnessed if a DGK was involved. Since PA kinase also uses ATP, a similar response in DGPP can be expected (panel D). Since the specific radioactivity of 32P-ATP decreases over time, the 1-min response decreases concomitantly. The combined assay is a relative measure and provides evidence for PA coming through DGK- and/or PLD pathways. See details in Arisz et al. , 2009 (Ref 68, 84) and in response to cold stress (ref 80).
Using Fluorescent-Protein (FP) fusions of specific lipid-binding domains, stably expressed in tobacco BY-2 cells and Arabidopsis, we have generated various lipid biosensor lines tthat can be used to topographically visualize where certain lipids are localised and/or generated. Currently, we have biosensors for PI3P (ref 28), PI4P (ref 62), PI(4,5)P2 (ref 55), PI(3,5)P2 (ref 107) and DAG (ref 106). Yvon Jaillais' lab (Lyon) recently characterized FP-sensors for PA and PS. In general, all biosensor lines are publically available.
Using T-DNA insertion mutants, evidence for the participation of individual PLC, PLD and DGK in stress signalling- & development is investigated. Arabidopsis contains 9 PLC-, 12 PLD- and 7 DGK genes. In addition, there are 11 PIP5K, 12 PI4K, 1 PI3K and multiple PA- and PPI phosphatase genes too. For many of them, we have mutants, which we are happy to share.
Below, an example of reduced salt tolerance for Arabidopsis pld mutants is shown. Seeds from wild-type (Col-0, black circles), pldα1 (open squares), pldδ (open triangles) or pldα1/pldδ double (open diamonds) knock-out mutant lines were sown on agar plates and grown vertically in a growth chamber. After 3 days seedlings were transferred to fresh plates supplemented with 0, 75 or 150 mM NaCl. Plates were scanned after 8 days (a) and primary root growth was followed and averaged ± SE during 4 days after transfer (b; n=12-16; a representative experiment is presented). (ref 63)
Polyphosphoinositides play distinct roles in membrane trafficking. This is examplified during cell divison, where PI3P, PI4P and PI(4,5)P2 exhibit distinct patterns when the new plasma membrane and cell wall that seperate the mother cell into two daughter cells, and the respective lipids were followed via genetically-encoded biosensors (green, YFP or red, mRFP for PI4P). The lipophylic dye, FM4-64 was used to stain membranes in general (red). While PI3P accumulates vesicles (late endosomes) surrounding the cell plate and is never part of the new plasma membrane (panel C), PI4P and DAG are always on the plasma membrane, right from the start when it is build (panel B, D), whereas PI(4,5)P2 is only present at the leading edges of the expanding cell plate (A).
Heat stress induces an array of physiological adjustments that facilitate continued homeostasis and survival during periods of elevated temperatures. Recently, we found that within minutes of a sudden temperature increase, plants rapidly produce PA and PIP2. Using a biosensor, we found that the heat-induced PIP2 is localized at the plasma membrane, nuclear envelope, nucleolus and at punctate cytoplasmic structures ( see below). Increases in steady-state levels of PA and PIP2 occured within several min of temperature increases from ambient levels of 20-25°C to 35°C and above. Similar patterns were observed in heat stressed Arabidopsis seedlings and rice leaves. The heat-induced results in large part from the activation of PLD rather than the sequential action of PLC and DGK. 32P-Pulse-labelling analysis revealed that the PIP2 response is due to activation of a PIPK rather than the inhibition of a lipase or PIP2 phosphatase (see ref 64, 69). Using T-DNA insertion mutants,. we are currenly identifying which of the 11 PIP5Ks and which of the 12 PLDs are involved. This work highly involves Michael Mishkind (NSF).
Osmotic stress responses not only involves salinity and drought but also hypotonic stress . Using 32Pi-labelling, specific PA and PPI responses have been uncovered (18, 21, 26, 29, 30, 40, 55). For the PPIs, different isomers are involved, which can be analyzed by lipid biosensors but also by HPLC analysis, using a strong anion-exchanger after deacylation, which generates so-called GroPIns' (see HPLC profile below).
At the moment, we are using lipid biosensor lines to find out where these lipid signals are generated, (55) and T-DNA insertion mutants to pinpoint the isoenzymes and genes are involved (63; Zarza et al., In prep).
PLC and PLD signalling cascades can individually generate PA, an important eukaryotic lipid second messenger. PLC generates it indirectly via the hydrolysis of PI(4,5)P2 and the subsequent phosphorylation of diacylglycerol (DAG) into PA via DAG kinase (DGK). PLD generates PA directly by hydrolyzing structural pospholipids, such as phosphatidylcholine (PC). Earlier, we have provided evidence for the role of PA in plant defence using elicitor-challenged cell suspensions of tomato, parsley and alfalfa. Currently, we are adressing PA's role genetically using the model system, Arabidopsis thaliana .
Arabidopsis contains 9 PLCs, 7 DGKs and 12 PLDs. To identify the genes involved in plant defence and characterise their individual functions, T-DNA insertion lines of most genes have been collected. Plants were then analysed for their disease resistance and sensitivity using virulent and avirulent strains of the bacterial pathogen, Pseudomonas syringae and the natural pathogen Hyaloperonospora parasitica , the causal agent of downy mildew. A DGK gene was found to be required for full resistance against virulent Pseudomonas and H. parasitica, while two PLD genes were found to be involved in the resistance against avirulent Pseudomonas (unpublished)
Work from Dr. Laura Zonia has focussed on one of the fastest growing cells on this planet: pollen tubes. The goal of this research is to identify key information cascades that control pollen tube growth and to understand how these networks link to the biomechanics that drive cell elongation. Several key cascades were identified, including actin cytoskeleton, ion fluxes and various phospholipid signals. Other workers have identified other cascades important for pollen tube growth, including GTPases, protein kinases, and processes involved in cell wall synthesis. Common themes emerging across these information cascades are osmoregulation and cell volume status. Further work confirmed that many of these networks indeed converge at this point, where we revealed that transcellular hydrodynamic flux drives the growth of a pollen tube and modulates rates of exocytosis and endocytosis.
Time-lapse images of tobacco pollen tubes double-labelled with FM 1-43 (green) and FM 4-64 (red) to identify sites of endocytosis and exocytosis and visualize membrane trafficking patterns. The first 3 images are from a pollen tube undergoing normal growth. The next 3 images are from a pollen tube undergoing hypertonic stress, which stimulates endocytic membrane retrieval at the apex and inhibits exocytosis. The last 2 images are from a pollen tube undergoing hypotonic stress, which stimulates exocytosis and growth, and attenuates endocytosis. Together with previous work (Zonia and Munnik, 2007), these data reveal that transcellular hydrodynamic flux is a key integrator of pollen tube growth, providing a motive force for cell elongation and regulating the rates of membrane insertion( exocytosis ) and retrieval (endocytosis). See refs 40, 49, 51, 53,57,60, 66.
Accumulating evidence suggests that PA plays a pivotal role in the plant's response to environmental signals. Besides PLD, PA can also be generated by DGK. To establish which metabolic route is activated, a differential 32P-labelling protocol can be used (see above). Based on this and on reverse-genetic approaches, DGK has taken center stage, next to PLD, as generator of PA in biotic- and abiotic-stress responses. The DAG substrate is generally thought to be derived from PLC activity. The model plant system Arabidopsis thaliana contains 7 DGKs, two of which, AtDGK1 and AtDGK2, resemble mammalian DGKε, encoding a conserved kinase domain, a transmembrane domain and two C1 domains. The other DGKs have a much simpler structure, lacking the C1 domains, not matched in animals. Several protein targets have been discovered to bind PA (Testerink and Munnik, 2011). Whether the PA comes from PLD or DGK often still remains to be elucidated. Cold stress, however, rapidly triggers PA via DGK within minutes (ref 107). Freezing stress involves PLDs (see Xuemin Wang Lab).
In comparison to mammals (which possess only two PLD genes) or yeast (one), plants possess a multitudinous and varied family of PLD genes. The genome of Arabidopsis thaliana contains twelve PLD family members and this diversity has been found in assorted higher plant species. PLD enzymes in eukaryotes are characterized by two highly conserved carboxy-terminal (C-terminal) catalytic domains and an amino-terminal (N-terminal) lipid-binding region (Figure). The two catalytic HxKxxxxD (HKD) motifs interact and are essential for the lipase activity of rat PLD1.
The plant PLD family can be divided into two sub-families, based on their N-terminal lipid-binding domains (see below). In Arabidopsis, two of the 12 PLDs contain a Phox homology- (PX) a pleckstrin homology (PH) domain, whereas the remaining 10 PLDs contain a C2 domain. PX and PH domains have been shown to mediate protein-membrane targeting and are closely linked to PPI signaling. C2 domains also mediate the localization of soluble proteins to membranes by binding lipids in a Ca2+-dependent manner. Importantly, PX, PH and C2 domains have also been implicated in protein-protein interactions. The plant-PLD family can be subdivided further into six classes, on the basis of sequence homology and in vitro enzymatic activity. The Arabidopsis genome contains three α-, two β-, three γ-, one δ-, one ε- and two ζ-class PLD isoforms; the latter class contains the PX and PH domains and shares more homology with yeast and mammalian PLDs than with other plant PLD classes.
PI-PLCs have been classified into six subfamilies, β, γ, δ, ε, η and ζ, based on domain structure and organization, (Figure; Munnik & Testerink, 2009). Mammalian cells contain all six isoforms (13 in total) whereas plants only exhibit one, i.e PLCζ-like, which is the class that lacks the Pleckstrin Homology (PH) domain present in all other PI-PLCs. In mammalian cells, PLCζ is specifically expressed in sperm cells.
PLCζ represents the most simple PI-PLC isoform, only consisting of the catalytic X- and Y-domain, an EF-hand domain and a C2 lipid-binding domain. Other subfamilies contain, besides the beforementioned domains, conserved sequences that allow them to be regulated by e.g. heterotrimeric G-proteins (PLCβ), tyrosine kinases (PLCγ), or Ras (PLCε). How PLCδ, -η and -ζ isoforms are regulated is unclear but may involve Ca2+.
Abbreviations: EF, EF-hand domain; PH, Pleckstrin homology domain; RA, Ras-binding domain; RasGEF, guanine-nucleotide-exchange factor for Ras; SH, Src homology domain; X and Y, catalytic domain.
Lipid Signaling in Plants . Series: Plant Cell Monographs,
Vol. 16 , Munnik, T. (Ed.) 2010, 330 p. 49 illus., 7 in
color., Hardcover. ISBN: 978-3-642-03872-3. Springer Verlag, Heidelberg,
Plant Lipid Signaling Protocols. Munnik T . and Heilmann I. ( Eds.) 2013. Series: Methods in Molecular Biology 1009, Humana Press, NJ, USA. 305 p.
1. De Nobel JG, Munnik T, Priem J, van den Ende H, Klis FM. (1990) Conditions for increased cell wall porosity in Yeast. Proceedings 3rdNetherlands Biotechnology Congress, Amsterdam, April 3-4, 1990. H Breteler, RF Beudeker and KChAM Luyben (Eds), pp. 300-304.
2. De Vrije T. & Munnik T. (1998) Signal Transduction pathways and senescence. In: The Post-Harvest Treatment of Fruit and Vegetables - Current Status and Future prospects. Eds. Woltering EJ, Gorris LG, Jongen WMF, McKenna B, Höhn E, Bertolini P, Woolfe ML, de Jager A, Ahvenainen R, Artes Calero F, Luxembourg, European Communities, pp 329-338 (ISBN 92-828-2003-3).
3. Testerink C. & Munnik T. (2004) Plant response to stress: phosphatidic acid as a second messenger. In Encyclopedia of Plant & Crop Science(RM Goodman, ed.), Marcel Dekker Inc, New York, 995-998.
4. De Wit PJGM, Brandwagt BF, van den Burg HA, Gabriëls SHEJ, van der Hoorn RAL, de Jong CF, van ‘t Klooster JW,de Kock MJD, Kruijt M, Luderer, R, Munnik T, Stulemeijer IJE, Thomma BPHJ, Vervoort JJM, Westerink N, Joosten MHAJ. (2004) Molecular basis of plant response to microbial invasion.In: Biology of Plant-Microbe Interactions, Vol. 4, Tikhonovich I, Lugtenberg B, Provorov N (Eds.), International Society for Molecular Plant-Microbe Interactions, St. Paul, Minnesota, USA, pp. 203-207.
5. Zonia L. & Munnik T. (2006) Cracking the green paradigm: Functional coding of phosphoinositide signals in plant stressresponses. In: Subcellular Biochemistry, Vol. 39:Biology of Inositols and Phosphoinositides (Majunder AL and Biswas BB, eds.), Kluwer/Plenum Publishers, London, UK, pp207-237.
6. Lee Y, Munnik T, Lee Y (2010) Plant Phosphatidylinositol 3-kinase. In Lipid Signaling in Plants. Series: Plant Cell Monographs, Vol. 16, Munnik, T. (Ed.), Springer-Verlag, Heidelberg, Germany, pp95-106.
7. Arisz SA and Munnik T. (2010) Diacylglycerol kinase. InLipid Signaling in Plants. Series: Plant Cell Monographs, Vol. 16, Munnik, T. (Ed.), Springer-Verlag, Heidelberg, Germany, pp107-114.
8. Vermeer JEM and Munnik T. (2010) Imaging lipids in living plants. In: Lipid Signaling in Plants. Series: Plant Cell Monographs, Vol. 16, Munnik T.(Ed.), Springer-Verlag, Heidelberg, Germany, pp185-199.
9. Munnik T. (2014) PI-PLC: Phosphoinositide-phospholipase C in plant signaling. In: Phospholipases in Plant Signaling. Wang X. (Ed.), Signaling and Communication in Plants 20, Springer-Verlag, Berlin Heidelberg. pp 27-54.
Stress Signalling - Signal transduction - Phospholipid signalling - Membrane trafficking - Abiotic Stress (cold, heat, drought, salt) - Biotic Stress (plant-pathogen) - Arabidopsis Development - Molecular Heaters
Cell Biology, Biochemistry, Plant Molecular Biology, Plant Physiology
• British Council Fellowship (1994)
• EMBO short-term Fellowship (1997)
• PULS Fellowship (1998-2001)
• KNAW (Dutch Royal Society of Sciences) Fellowship (2000-2005)
• VIDI fellowship for innovative research (2005-2010)
• ECHO grant (2007)
• VPP grant (2011)
• NPST grant (2012)
• NWO-DBT grant (2015-2020)
• ECHO grant (2018-2021)
• IXA grant (2018)
• EU-FET grant (2019)
Publications: (see All Publications)
• Number of publications in international refereed scientific journals according to WoS: 119
• Contributions to books:
- 2 books (Ed. 2010; Ed. 2013, both Springer);
- 7 chapters
• Number of citations according to WoS: >8400; average citations: 72; H-index: 55
• Lecturer at various International Advanced Courses (e.g. ICRO; FEBS, EPS, UNMP, TWAS)
• Coordinator and teacher of various BSc, MSc and PhD courses (molecular cell biology, biochemistry, cellular physiology, plant-abiotic stress)
• >150 Invited seminars at (inter)national universities, conferences and symposia, world wide (see below).
• Organiser of seminars for SILS, University of Amsterdam
• Organiser of Plant & Green Life Science seminars at SILS, GLS, University of Amsterdam
• Conference chair at various national- and international conferences
• Organiser & chair of Gordon Research Conference (GRC) Salt and Water Stress 2012, Hong Kong, China.
• Co-organiser of the 15th World Conference of Parasitic Plants (WCPP2019), Amsterdam, The Netherlands.
• Organiser of the 10th ESPL, European Symposium on Plant Lipids (2021), Amsterdam, The Netherlands.
Currently, no vacancies
(e.g. FEBS, EMBO, Marie Curie, etc) - please contact: t.munnik @ uva.nl
Phosphatidic acid (PA) and polyphosphoinositides (PPIs) are minor phospholipids in biological membranes that function as cellular signalling molecules at very low concentrations. Their turnover is much faster than of structural phospholipids and levels quickly change in response to biotic- (pathogens) and abiotic- (salt, cold, heat, drought) stresses. How this is regulated and where this occurs in the cell (e.g. plasma membrane, ER, Golgi) or in the whole plant (e.g. root, stem, stomata) has our particular interest. The genome of the model plant system Arabidopsis thaliana, encodes genes for various lipid kinases, phosphatases and phospholipases, and by using T-DNA insertion knock-out mutants, overexpression lines, and FP fusions, we are pinpointing their individual contribution in stress and/or development. Over the years we constructed various lipid biosensor lines, which are plants expressing specific lipid-binding domains that are fused to a fluorescent protein that are used to study the dynamics of lipid-second messengers in living cells. Personal felowships or students can be involved in any of the projects.
Teun Munnik (PI)
Ing. Ringo van Wijk (Lab manager)
Dr. Xavier Zarza (Post-doc)
Dr. Femke de Jong (Post-doc)
Dr. Steven Arisz (senior Post-doc)
Drs. Max van Hooren (PhD student)
Ms Hui Sheng (PhD student)
Mrs. Safrina Ahmad (PhD student)
Drs. Xandra Schrama (technician)
Drs. Floris Stevens (technician)
Drs. Stella Prelovšek (technician)
Dr. Michael Mishkind (permanent guest)
Dr. Leonardo Hinojosa (guest)
Laura Zonia (Washington University in St. Louis, MO, USA)
Aleksandra Haduch (PhD student, Poland)
Wendy Roels (Naktuinbouw)
Dörte Klaus (PD, Toulouse, F)
Christiane Unger (MSc, Halle, Germany)
Alan Musgrave (UvA, retired)
Ana Laxalt (PI, Mar del Plata, Argentina)
Bas ter Riet (Enza Zaden, Enkhuizen, NL)
Harold Meijer (WUR, Wageningen, NL)
Christa Testerink (Prof. Plant Physiology, WUR)
Wessel van Leeuwen (Hazera Seeds, NL)
Rafa Tobeña (Madrid, Spain)
Gert-Jan de Boer (Enza Zaden, Enkhuizen, NL)
John van Himbergen (VROM)
Diewertje van der Does (UU, Utrecht, NL)
Saskia van Wees (UU, Utrecht, NL)
Fabio Formiggini (Italy)
Gaby Gonorazky (Uni of Mar del Plata, Argentina)
Martine den Hartog (Covidien, Amsterdam)
Arnold van der Luit (Oncodesign, France)
Bastiaan Bargmann (CA, USA)
Bas van Schooten (NWO)
Essam Darwish (Uni. Cairo, Egypt)
Joop Vermeer (Prof. Plant Cell Biology, Uni of Zürich, Switzerland)
Muhammad Shahbaz (Prof. Uni of Faisalabad, Pakistan)
Qianqian Zhang (Nikon, Shanghai, China)
Jessica Meyer (technician WUR)
Nazish Annum (Agricultural Biotechnogy Division, National Institute for Biotechnology and Genetic Enginering, Faisalabad, Pakistan)
Ruud Korver (ENZA)
Mhyrte Praat (Utrecht University)
Martine den Hartog
Julian C. Verdonk
Steven A. Arisz
Bas ter Riet
Diewertje van der Does
Jacco van Rheenen
Carlos Jr. Rubio 'Chucho'
Mark aan 't Goor
Martijn van Ophem
Rui Alvez (Erasmus student)
Babette Vlieger (BSc student)
Ludo Cialdella (BSc student)
Jack Dickenson (MSc student)
Eveline Bosman (BSc student)
Valerie de Ridder (BSc student)
Dr. Michael Mishkind (NSF, VA, USA)
Dr. Ana Laxalt (Mar del Plata, Argentina)
Dr. Joachim Goedhart (WU, Wageningen)
Dr. Dorus Gadella (WU, Wageningen)
Dr. Bas Tomassen (Erasmus Rotterdam, NL)
Dr. Katie Anne Wilkins (Birmingham, UK)
Dr. Anne Sophie Leprince (Paris, France)
Dr. Noam Reznik (Tel Aviv, Israel)
Dr. Magdalena Wierzchowiecka (Poland)
MSc. Özgecan Tanyolaç (Izmir, Turkey)
MSc. Maria Alejandra Schlöffel (University of Tübingen, Germany)
Dr. Bojan Gujas (ETH, Zürich, Switzerland)
Dr. Necla Pehlivan (Turkey)
Dr. Theodora Farmaki, (Thessaloniki, Greece)
Dr. Wojciech Rymaszewski (Warsaw, Poland)
Dr. Hui-fen Kuo (Academia Sinica, Taiwan)
Dr. Kelly Stecker (University of Wisconsin, USA)
Dr. Muhammad Jamil (WUR)
MSc Madiha Butt (Faisalabad, Pakistan)
Dr. Tomoko Hirano (Kyoto Prefectural University, Japan)
Dr. Jyothilakshmi Vadassery (Max Planck, Germany)
MSc. Dominik Novák (Palacky University, Olomouc, Czech Republic)
Dorus Gadella (SILS, UvA, NL)
Nullin Divecha (Manchester, UK)
Mats Ellerström (Göteborg University, Sweden)
Takashi Aoyama (Kyoto University, Japan)
Erik Nielsen (Michigan, US)
Ana Laxalt (University of Mar del Plata, Argentina)
Charles Brearley (Norwich, UK)
Gertjan Kramer (SILS, UvA, NL)
Harro Bouwmeester (SILS, UvA, NL)
Ingo Heilmann (Halle, Germany)
Robin Irvine (Cambridge, UK, retired)
Laura de la Canal (Mar del Plata, Argentina)
Nick Ktistakis (Cambridge, UK)
Ralf Oelmüller (Jena, Germany)
Jack Vossen (WUR, Wageningen, NL)
Gerard van der Linden (WUR, Wageningen, NL)
Dierk Scheel (Halle, Germany)
Dorothea Bartels (Bonn, Germany)
George Carman (Rutgers, NJ, US)
Laci Bögre (London, UK)
Claudia Jonak (Vienna, Austria)
Susanne Hoffmann-Benning (Michigan, US)
Pavla Binarova (Prague, Czech Republic)
Jörg Kudla (Münster, Germany)
Silke Robatzek (Münich, Germany)
Mariusz Pietruszka (University of Silesia, Poland)
Antonio Fernandez Tiburcio (Barcelona, Spain)
Noni Franklin-Tong (University of Birmingham, UK)
Edgar Kooijman (Kent, USA)
Aviah Zilberstein (Tel Aviv, Israel)
İsmail Türkan (Izmir, Turkey)
Pia Harryson (Stockholm, Sweden)
Tzyy-Jen Chiou (Academia Sinica, Taiwan)
Libo Shan (Texas A&M University, US)
Ping He (Texas A&M University, US)
Glenda Gillaspy (Virginia Tech, US)
Yee-yung Charng (Academia Sinica, Taiwan)
Taijoon Chung (Pusan National University, Republic of Korea)
Jenny Russinova (VIB, Ghent University, Belgium)
Gabriel Schaaf (University of Bonn, Germany)
Luis Lopez-Molina (University of Geneva, Switzerland)
Antia Rodriguez-Villalon (ETH, Zürich, Sitzerland)
Christian S. Hardtke (Lausanne, Sitzerland)
Niko Geldner (Uni Lausanne, Sitzerland)
Joop Vermeer (Uni Zürich, Sitzerland)
Wybren Jan Buma (HIMS,Molecular photonics UvA)
Jan van Maarseveen (HIMS, Organisc chemistry, UvA)
Jiri Friml (IST Austria)