@book{KubanRottaNolteetal.2023, author = {Kuban, Robert and Rotta, Randolf and Nolte, J{\"o}rg and Chromik, Jonas and Beilharz, Jossekin Jakob and Pirl, Lukas and Friedrich, Tobias and Lenzner, Pascal and Weyand, Christopher and Juiz, Carlos and Bermejo, Belen and Sauer, Joao and Coelh, Leandro dos Santos and Najafi, Pejman and P{\"u}nter, Wenzel and Cheng, Feng and Meinel, Christoph and Sidorova, Julia and Lundberg, Lars and Vogel, Thomas and Tran, Chinh and Moser, Irene and Grunske, Lars and Elsaid, Mohamed Esameldin Mohamed and Abbas, Hazem M. and Rula, Anisa and Sejdiu, Gezim and Maurino, Andrea and Schmidt, Christopher and H{\"u}gle, Johannes and Uflacker, Matthias and Nozza, Debora and Messina, Enza and Hoorn, Andr{\´e} van and Frank, Markus and Schulz, Henning and Alhosseini Almodarresi Yasin, Seyed Ali and Nowicki, Marek and Muite, Benson K. and Boysan, Mehmet Can and Bianchi, Federico and Cremaschi, Marco and Moussa, Rim and Abdel-Karim, Benjamin M. and Pfeuffer, Nicolas and Hinz, Oliver and Plauth, Max and Polze, Andreas and Huo, Da and Melo, Gerard de and Mendes Soares, F{\´a}bio and Oliveira, Roberto C{\´e}lio Lim{\~a}o de and Benson, Lawrence and Paul, Fabian and Werling, Christian and Windheuser, Fabian and Stojanovic, Dragan and Djordjevic, Igor and Stojanovic, Natalija and Stojnev Ilic, Aleksandra and Weidmann, Vera and Lowitzki, Leon and Wagner, Markus and Ifa, Abdessatar Ben and Arlos, Patrik and Megia, Ana and Vendrell, Joan and Pfitzner, Bjarne and Redondo, Alberto and R{\´i}os Insua, David and Albert, Justin Amadeus and Zhou, Lin and Arnrich, Bert and Szab{\´o}, Ildik{\´o} and Fodor, Szabina and Ternai, Katalin and Bhowmik, Rajarshi and Campero Durand, Gabriel and Shevchenko, Pavlo and Malysheva, Milena and Prymak, Ivan and Saake, Gunter}, title = {HPI Future SOC Lab - Proceedings 2019}, number = {158}, editor = {Meinel, Christoph and Polze, Andreas and Beins, Karsten and Strotmann, Rolf and Seibold, Ulrich and R{\"o}dszus, Kurt and M{\"u}ller, J{\"u}rgen}, publisher = {Universit{\"a}tsverlag Potsdam}, address = {Potsdam}, isbn = {978-3-86956-564-4}, issn = {1613-5652}, doi = {10.25932/publishup-59791}, url = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-597915}, publisher = {Universit{\"a}t Potsdam}, pages = {xi, 301}, year = {2023}, abstract = {The "HPI Future SOC Lab" is a cooperation of the Hasso Plattner Institute (HPI) and industry partners. Its mission is to enable and promote exchange and interaction between the research community and the industry partners. The HPI Future SOC Lab provides researchers with free of charge access to a complete infrastructure of state of the art hard and software. This infrastructure includes components, which might be too expensive for an ordinary research environment, such as servers with up to 64 cores and 2 TB main memory. The offerings address researchers particularly from but not limited to the areas of computer science and business information systems. Main areas of research include cloud computing, parallelization, and In-Memory technologies. This technical report presents results of research projects executed in 2019. Selected projects have presented their results on April 9th and November 12th 2019 at the Future SOC Lab Day events.}, language = {en} } @article{SauerGrebe2021, author = {Sauer, Michael and Grebe, Markus}, title = {Plant cell biology}, series = {Current biology : CB}, volume = {31}, journal = {Current biology : CB}, number = {9}, publisher = {Cell Press}, address = {Cambridge}, issn = {0960-9822}, doi = {10.1016/j.cub.2021.03.070}, pages = {R449 -- R451}, year = {2021}, abstract = {PIN-FORMED (PIN) polar protein localization directs transport of the growth and developmental regulator auxin in plants. Once established after cytokinesis, PIN polarity requires maintenance. Now, direct interactions between PIN, MAB4/MEL and PID proteins suggest self-reinforced maintenance of PIN polarity through limiting lateral diffusion.}, language = {en} } @article{WartenbergLingMueschenetal.2003, author = {Wartenberg, Maria and Ling, Frederike C. and M{\"u}schen, Markus and Klein, Florian and Acker, Helmut and Gassmann, Max and Petrat, Kerstin and P{\"u}tz, Volker and Hescheler, J{\"u}rgen and Sauer, Heinrich}, title = {Regulation of the multidrug resistance transporter P-glycorotein by hypoxia-inducible factor (HIF-1) and reactive oxygen species}, year = {2003}, language = {en} } @article{KleinFeldhahnLeeetal.2003, author = {Klein, Florian and Feldhahn, Niklas and Lee, Sanggyu and Wang, Hui and Ciuffi, Fiammetta and von Elstermann, Mirko and Toribio, Maria L. and Sauer, Heinrich and Wartenberg, Maria and Barath, Varun Singh and Kr{\"o}nke, Martin and Wernet, Peter and Rowley, Janet D. and M{\"u}schen, Markus}, title = {T lymphoid differentiation in human bone marrow}, year = {2003}, language = {en} } @misc{PratHajnýGrunewaldetal.2018, author = {Pr{\´a}t, Tom{\´a}š and Hajny', Jakub and Grunewald, Wim and Vasileva, Mina and Moln{\´a}r, Gergely and Tejos, Ricardo and Schmid, Markus and Sauer, Michael and Friml, Jiř{\´i}}, title = {WRKY23 is a component of the transcriptional network mediating auxin feedback on PIN polarity}, series = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe}, journal = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe}, number = {1123}, issn = {1866-8372}, doi = {10.25932/publishup-44633}, url = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-446331}, pages = {20}, year = {2018}, abstract = {Auxin is unique among plant hormones due to its directional transport that is mediated by the polarly distributed PIN auxin transporters at the plasma membrane. The canalization hypothesis proposes that the auxin feedback on its polar flow is a crucial, plant-specific mechanism mediating multiple self-organizing developmental processes. Here, we used the auxin effect on the PIN polar localization in Arabidopsis thaliana roots as a proxy for the auxin feedback on the PIN polarity during canalization. We performed microarray experiments to find regulators of this process that act downstream of auxin. We identified genes that were transcriptionally regulated by auxin in an AXR3/IAA17-and ARF7/ARF19-dependent manner. Besides the known components of the PIN polarity, such as PID and PIP5K kinases, a number of potential new regulators were detected, among which the WRKY23 transcription factor, which was characterized in more detail. Gain-and loss-of-function mutants confirmed a role for WRKY23 in mediating the auxin effect on the PIN polarity. Accordingly, processes requiring auxin-mediated PIN polarity rearrangements, such as vascular tissue development during leaf venation, showed a higher WRKY23 expression and required the WRKY23 activity. Our results provide initial insights into the auxin transcriptional network acting upstream of PIN polarization and, potentially, canalization-mediated plant development.}, language = {en} } @article{PratHajnyGrunewaldetal.2018, author = {Prat, Tomas and Hajny, Jakub and Grunewald, Wim and Vasileva, Mina and Molnar, Gergely and Tejos, Ricardo and Schmid, Markus and Sauer, Michael and Friml, Jiř{\´i}}, title = {WRKY23 is a component of the transcriptional network mediating auxin feedback on PIN polarity}, series = {PLoS Genetics : a peer-reviewed, open-access journal}, volume = {14}, journal = {PLoS Genetics : a peer-reviewed, open-access journal}, number = {1}, publisher = {PLoS}, address = {San Fransisco}, issn = {1553-7404}, doi = {10.1371/journal.pgen.1007177}, pages = {18}, year = {2018}, abstract = {Auxin is unique among plant hormones due to its directional transport that is mediated by the polarly distributed PIN auxin transporters at the plasma membrane. The canalization hypothesis proposes that the auxin feedback on its polar flow is a crucial, plant-specific mechanism mediating multiple self-organizing developmental processes. Here, we used the auxin effect on the PIN polar localization in Arabidopsis thaliana roots as a proxy for the auxin feedback on the PIN polarity during canalization. We performed microarray experiments to find regulators of this process that act downstream of auxin. We identified genes that were transcriptionally regulated by auxin in an AXR3/IAA17-and ARF7/ARF19-dependent manner. Besides the known components of the PIN polarity, such as PID and PIP5K kinases, a number of potential new regulators were detected, among which the WRKY23 transcription factor, which was characterized in more detail. Gain-and loss-of-function mutants confirmed a role for WRKY23 in mediating the auxin effect on the PIN polarity. Accordingly, processes requiring auxin-mediated PIN polarity rearrangements, such as vascular tissue development during leaf venation, showed a higher WRKY23 expression and required the WRKY23 activity. Our results provide initial insights into the auxin transcriptional network acting upstream of PIN polarization and, potentially, canalization-mediated plant development.}, language = {en} } @article{CollenburgWalterBurgertetal.2016, author = {Collenburg, Lena and Walter, Tim and Burgert, Anne and Mueller, Nora and Seibel, Juergen and Japtok, Lukasz and Kleuser, Burkhard and Sauer, Markus and Schneider-Schaulies, Sibylle}, title = {A Functionalized Sphingolipid Analogue for Studying Redistribution during Activation in Living T Cells}, series = {The journal of immunology}, volume = {196}, journal = {The journal of immunology}, publisher = {American Assoc. of Immunologists}, address = {Bethesda}, issn = {0022-1767}, doi = {10.4049/jimmunol.1502447}, pages = {3951 -- 3962}, year = {2016}, abstract = {Sphingolipids are major components of the plasma membrane. In particular, ceramide serves as an essential building hub for complex sphingolipids, but also as an organizer of membrane domains segregating receptors and signalosomes. Sphingomyelin breakdown as a result of sphingomyelinase activation after ligation of a variety of receptors is the predominant source of ceramides released at the plasma membrane. This especially applies to T lymphocytes where formation of ceramide-enriched membrane microdomains modulates TCR signaling. Because ceramide release and redistribution occur very rapidly in response to receptor ligation, novel tools to further study these processes in living T cells are urgently needed. To meet this demand, we synthesized nontoxic, azido-functionalized ceramides allowing for bio-orthogonal click-reactions to fluorescently label incorporated ceramides, and thus investigate formation of ceramide-enriched domains. Azido-functionalized C-6-ceramides were incorporated into and localized within plasma membrane microdomains and proximal vesicles in T cells. They segregated into clusters after TCR, and especially CD28 ligation, indicating efficient sorting into plasma membrane domains associated with T cell activation; this was abolished upon sphingomyelinase inhibition. Importantly, T cell activation was not abrogated upon incorporation of the compound, which was efficiently excluded from the immune synapse center as has previously been seen in Ab-based studies using fixed cells. Therefore, the functionalized ceramides are novel, highly potent tools to study the subcellular redistribution of ceramides in the course of T cell activation. Moreover, they will certainly also be generally applicable to studies addressing rapid stimulation-mediated ceramide release in living cells.}, language = {en} } @article{DerakhshaniKurzJaptoketal.2019, author = {Derakhshani, Shaghayegh and Kurz, Andreas and Japtok, Lukasz and Schumacher, Fabian and Pilgram, Lisa and Steinke, Maria and Kleuser, Burkhard and Sauer, Markus and Schneider-Schaulies, Sibylle and Avota, Elita}, title = {Measles Virus Infection Fosters Dendritic Cell Motility in a 3D Environment to Enhance Transmission to Target Cells in the Respiratory Epithelium}, series = {Frontiers in immunology}, volume = {10}, journal = {Frontiers in immunology}, publisher = {Frontiers Research Foundation}, address = {Lausanne}, issn = {1664-3224}, doi = {10.3389/fimmu.2019.01294}, pages = {14}, year = {2019}, abstract = {Transmission of measles virus (MV) from dendritic to airway epithelial cells is considered as crucial to viral spread late in infection. Therefore, pathways and effectors governing this process are promising targets for intervention. To identify these, we established a 3D respiratory tract model where MV transmission by infected dendritic cells (DCs) relied on the presence of nectin-4 on H358 lung epithelial cells. Access to recipient cells is an important prerequisite for transmission, and we therefore analyzed migration of MV-exposed DC cultures within the model. Surprisingly, enhanced motility toward the epithelial layer was observed for MV-infected DCs as compared to their uninfected siblings. This occurred independently of factors released from H358 cells indicating that MV infection triggered cytoskeletal remodeling associated with DC polarization enforced velocity. Accordingly, the latter was also observed for MV-infected DCs in collagen matrices and was particularly sensitive to ROCK inhibition indicating infected DCs preferentially employed the amoeboid migration mode. This was also implicated by loss of podosomes and reduced filopodial activity both of which were retained in MV-exposed uninfected DCs. Evidently, sphingosine kinase (SphK) and sphingosine-1-phosphate (S1P) as produced in response to virus-infection in DCs contributed to enhanced velocity because this was abrogated upon inhibition of sphingosine kinase activity. These findings indicate that MV infection promotes a push-and-squeeze fast amoeboid migration mode via the SphK/S1P system characterized by loss of filopodia and podosome dissolution. Consequently, this enables rapid trafficking of virus toward epithelial cells during viral exit.}, language = {en} } @article{FinkSchumacherSchlegeletal.2021, author = {Fink, Julian and Schumacher, Fabian and Schlegel, Jan and Stenzel, Philipp and Wigger, Dominik and Sauer, Markus and Kleuser, Burkhard and Seibel, J{\"u}rgen}, title = {Azidosphinganine enables metabolic labeling and detection of sphingolipid de novo synthesis}, series = {Organic \& biomolecular chemistry : an international journal of synthetic, physical and biomolecular organic chemistry}, volume = {19}, journal = {Organic \& biomolecular chemistry : an international journal of synthetic, physical and biomolecular organic chemistry}, number = {10}, publisher = {Royal Society of Chemistry}, address = {Cambridge}, issn = {1477-0520}, doi = {10.1039/d0ob02592e}, pages = {2203 -- 2212}, year = {2021}, abstract = {Here were report the combination of biocompatible click chemistry of omega-azidosphinganine with fluorescence microscopy and mass spectrometry as a powerful tool to elaborate the sphingolipid metabolism. The azide probe was efficiently synthesized over 13 steps starting from l-serine in an overall yield of 20\% and was used for live-cell fluorescence imaging of the endoplasmic reticulum in living cells by bioorthogonal click reaction with a DBCO-labeled fluorophore revealing that the incorporated analogue is mainly localized in the endoplasmic membrane like the endogenous species. A LC-MS(/MS)-based microsomal in vitro assay confirmed that omega-azidosphinganine mimics the natural species enabling the identification and analysis of metabolic breakdown products of sphinganine as a key starting intermediate in the complex sphingolipid biosynthetic pathways. Furthermore, the sphinganine-fluorophore conjugate after click reaction was enzymatically tolerated to form its dihydroceramide and ceramide metabolites. Thus, omega-azidosphinganine represents a useful biofunctional tool for metabolic investigations both by in vivo fluorescence imaging of the sphingolipid subcellular localization in the ER and by in vitro high-resolution mass spectrometry analysis. This should reveal novel insights of the molecular mechanisms sphingolipids and their processing enzymes have e.g. in infection.}, language = {en} }