Options
Heilmann, Ingo
Loading...
Preferred name
Heilmann, Ingo
Official Name
Heilmann, Ingo
Alternative Name
Heilmann, I.
Now showing 1 - 8 of 8
2008Journal Article [["dc.bibliographiccitation.firstpage","249"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Molecular Plant"],["dc.bibliographiccitation.lastpage","261"],["dc.bibliographiccitation.volume","1"],["dc.contributor.author","Mosblech, Alina"],["dc.contributor.author","Koenig, Sabine"],["dc.contributor.author","Stenzel, Irene"],["dc.contributor.author","Grzeganek, Peter"],["dc.contributor.author","Feussner, Ivo"],["dc.contributor.author","Heilmann, Ingo"],["dc.date.accessioned","2018-11-07T11:17:53Z"],["dc.date.available","2018-11-07T11:17:53Z"],["dc.date.issued","2008"],["dc.description.abstract","Various biochemical signals are implicated in Arabidopsis wound signalling, including jasmonic acid (JA), salicylic acid, auxin, and Ca2+. Here, we report on cross-talk of phytohormones with phosphoinositide signals not previously implicated in plant wound responses. Within 30 min of mechanical wounding of Arabidopsis rosette-leaves, the levels of the lipid-derived soluble inositolpolyphosphate, inositol 1,4,5-trisphosphate (InsP(3)), increased four to five-fold. Concomitantly, the precursor lipids, phosphatidylinositol 4,5-bisphosphate, phosphatidylinositol 4-phosphate and phosphatidylinositol transiently depleted, followed by re-synthesis after 30-60 min of stimulation. Increased InsP(3) levels with wounding coincided with JA increases over the first hours of stimulation. In dde2-2-mutant plants deficient in JA biosynthesis, no InsP(3) increase was observed upon wounding, indicating that JA was required for InsP(3) formation, and InsP(3) levels increased in wild-type plants challenged with sorbitol, increasing endogenous JA levels. In InsP 5-ptase plants with attenuated phosphoinositide signalling, the induction of wounding-inducible genes was diminished compared with wildtype plants, suggesting a role for phosphoinositide signalling in mediating plant wound responses. The gene-expression patterns suggest that phosphoinositides contribute to both JA-dependent and JA-independent aspects of wound signalling. Weight gain of Plutella xylostella caterpillars feeding on InsP 5-ptase plants was increased compared with that of caterpillars feeding on wild-type plants. The ecophysiological relevance of phosphoinositide signals in plant defense responses to herbivory is discussed in light of recent findings of inositolpolyphosphate involvement in phytohormone-receptor function."],["dc.description.sponsorship","German Research Foundation [He3424/1-3]"],["dc.identifier.doi","10.1093/mp/ssm028"],["dc.identifier.isi","000259103700006"],["dc.identifier.pmid","19825537"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/54919"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Oxford Univ Press"],["dc.relation.issn","1674-2052"],["dc.title","Phosphoinositide and inositolpolyphosphate signalling in defense responses of Arabidopsis thaliana challenged by mechanical wounding"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2013Journal Article [["dc.bibliographiccitation.firstpage","4894"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","The Plant Cell"],["dc.bibliographiccitation.lastpage","4911"],["dc.bibliographiccitation.volume","25"],["dc.contributor.author","Ischebeck, Till"],["dc.contributor.author","Werner, Stephanie"],["dc.contributor.author","Krishnamoorthy, Praveen"],["dc.contributor.author","Lerche, Jennifer"],["dc.contributor.author","Meijon, Monica"],["dc.contributor.author","Stenzel, Irene"],["dc.contributor.author","Loefke, Christian"],["dc.contributor.author","Wiessner, Theresa"],["dc.contributor.author","Im, Yang Ju"],["dc.contributor.author","Perera, Imara Y."],["dc.contributor.author","Iven, Tim"],["dc.contributor.author","Feussner, Ivo"],["dc.contributor.author","Busch, Wolfgang"],["dc.contributor.author","Boss, Wendy F."],["dc.contributor.author","Teichmann, Thomas"],["dc.contributor.author","Hause, Bettina"],["dc.contributor.author","Persson, Staffan"],["dc.contributor.author","Heilmann, Ingo"],["dc.date.accessioned","2018-11-07T09:16:43Z"],["dc.date.available","2018-11-07T09:16:43Z"],["dc.date.issued","2013"],["dc.description.abstract","The functions of the minor phospholipid phosphatidylinositol-4,5-bisphosphate [PtdIns(4,5)P-2] during vegetative plant growth remain obscure. Here, we targeted two related phosphatidylinositol 4-phosphate 5-kinases (PI4P 5-kinases) PIP5K1 and PIP5K2, which are expressed ubiquitously in Arabidopsis thaliana. A pip5k1 pip5k2 double mutant with reduced PtdIns(4,5)P-2 levels showed dwarf stature and phenotypes suggesting defects in auxin distribution. The roots of the pip5k1 pip5k2 double mutant had normal auxin levels but reduced auxin transport and altered distribution. Fluorescence-tagged auxin efflux carriers PIN-FORMED (PIN1)-green fluorescent protein (GFP) and PIN2-GFP displayed abnormal, partially apolar distribution. Furthermore, fewer brefeldin A-induced endosomal bodies decorated by PIN1-GFP or PIN2-GFP formed in pip5k1 pip5k2 mutants. Inducible overexpressor lines for PIP5K1 or PIP5K2 also exhibited phenotypes indicating misregulation of auxin-dependent processes, and immunolocalization showed reduced membrane association of PIN1 and PIN2. PIN cycling and polarization require clathrin-mediated endocytosis and labeled clathrin light chain also displayed altered localization patterns in the pip5k1 pip5k2 double mutant, consistent with a role for PtdIns(4,5)P-2 in the regulation of clathrin-mediated endocytosis. Further biochemical tests on subcellular fractions enriched for clathrin-coated vesicles (CCVs) indicated that pip5k1 and pip5k2 mutants have reduced CCV-associated PI4P 5-kinase activity. Together, the data indicate an important role for PtdIns(4,5)P-2 in the control of clathrin dynamics and in auxin distribution in Arabidopsis."],["dc.identifier.doi","10.1105/tpc.113.116582"],["dc.identifier.isi","000330611200014"],["dc.identifier.pmid","24326589"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/27998"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Plant Biologists"],["dc.relation.issn","1532-298X"],["dc.relation.issn","1040-4651"],["dc.title","Phosphatidylinositol 4,5-Bisphosphate Influences PIN Polarization by Controlling Clathrin-Mediated Membrane Trafficking in Arabidopsis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2009Conference Paper [["dc.bibliographiccitation.firstpage","511"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Plant Physiology and Biochemistry"],["dc.bibliographiccitation.lastpage","517"],["dc.bibliographiccitation.volume","47"],["dc.contributor.author","Mosblech, Alinal"],["dc.contributor.author","Feussner, Ivo"],["dc.contributor.author","Heilmann, Ingo"],["dc.date.accessioned","2018-11-07T08:29:36Z"],["dc.date.available","2018-11-07T08:29:36Z"],["dc.date.issued","2009"],["dc.description.abstract","Oxylipins are lipophilic signaling molecules derived from the oxidation of polyunsaturated fatty acids. Initial fatty acid oxidation occurs mainly by the enzymatic or chemical formation of fatty acid hydroperoxides. An array of alternative reactions further converting fatty acid hydroperoxides gives rise to a multitude of oxylipin classes, many with reported signaling functions in plants. Oxylipins include the phytohormone, jasmonic acid, and a number of other molecules including hydroxy-, oxo- or keto-fatty acids or volatile aldehydes that may perform various biological roles as second messengers, messengers in inter-organismic signaling, or even as bactericidal agents. The structural diversity of oxylipins is further increased by esterification of the compounds in plastidial glycolipids, for instance the Arabidopsides, or by conjugation of oxylipins to amino acids or other metabolites. The enzymes involved in oxylipin metabolism are diverse and comprise a multitude of examples with interesting and unusual catalytic properties. In addition, the interplay of different subcellular compartments during oxylipin biosynthesis suggests complex mechanisms of regulation that are not well understood. This review aims at giving an overview of plant oxylipins and the multitude of enzymes responsible for their biosynthesis. (C) 2008 Elsevier Masson SAS. All rights reserved."],["dc.identifier.doi","10.1016/j.plaphy.2008.12.011"],["dc.identifier.isi","000266272900011"],["dc.identifier.pmid","19167233"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/16690"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier France-editions Scientifiques Medicales Elsevier"],["dc.publisher.place","Paris"],["dc.relation.conference","18th Biennial International Symposium on Plant Lipids (ISPL)"],["dc.relation.eventlocation","Bordeaux, FRANCE"],["dc.relation.issn","0981-9428"],["dc.title","Oxylipins: Structurally diverse metabolites from fatty acid oxidation"],["dc.type","conference_paper"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2011Journal Article [["dc.bibliographiccitation.firstpage","949"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","The Plant Journal"],["dc.bibliographiccitation.lastpage","957"],["dc.bibliographiccitation.volume","65"],["dc.contributor.author","Mosblech, Alina"],["dc.contributor.author","Thurow, Corinna"],["dc.contributor.author","Gatz, Christiane"],["dc.contributor.author","Feussner, Ivo"],["dc.contributor.author","Heilmann, Ingo"],["dc.date.accessioned","2018-11-07T08:59:06Z"],["dc.date.available","2018-11-07T08:59:06Z"],["dc.date.issued","2011"],["dc.description.abstract","Plant responses to wounding are part of their defense responses against insects, and are tightly regulated. The isoleucin conjugate of jasmonic acid (JA-IIe) is a major regulatory molecule. We have previously shown that inositol polyphosphate signals are required for defense responses in Arabidopsis; however, the way in which inositol polyphosphates contribute to plant responses to wounding has so far remained unclear. Arabidopsis F-box proteins involved in the perception of JA-IIe (COI1) and auxin (TIR1) are structurally similar. Because TIR1 has recently been shown to contain inositol hexakisphosphate (InsP(6)) as a co-factor of unknown function, here we explored the possibility that InsP(6) or another inositol polyphosphate is required for COI1 function. In support of this hypothesis, COI1 variants with changes in putative inositol polyphosphate coordinating residues exhibited a reduced interaction with the COI1 target, JAZ9, in yeast two-hybrid tests. The equivalent COI1 variants displayed a reduced capability to rescue jasmonate-mediated root growth inhibition or silique development in Arabidopsis col1 mutants. Yeast two-hybrid tests using wild-type COI1 in an ipk1 Delta yeast strain exhibiting increased levels of inositol pentakisphosphate (InsP(5)) and reduced levels of InsP(6) indicate an enhanced COI1/JAZ9 interaction. Consistent with these findings, Arabidopsis ipk1-1 mutants, also with increased InsP(5) and reduced InsP(6) levels, showed increased defensive capabilities via COI1-mediated processes, including wound-induced gene expression, defense against caterpillars or root growth inhibition by jasmonate. The combined data from experiments using mutated COI1 variants, as well as yeast and Arabidopsis backgrounds altered in inositol polyphosphate metabolism, indicate that an inositol polyphosphate, and probably InsP(5), contributes to COI1 function."],["dc.identifier.doi","10.1111/j.1365-313X.2011.04480.x"],["dc.identifier.isi","000288449700009"],["dc.identifier.pmid","21205029"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/23810"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","0960-7412"],["dc.title","Jasmonic acid perception by COI1 involves inositol polyphosphates in Arabidopsis thaliana"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2008Journal Article [["dc.bibliographiccitation.firstpage","347"],["dc.bibliographiccitation.journal","Biochemical Journal"],["dc.bibliographiccitation.lastpage","357"],["dc.bibliographiccitation.volume","410"],["dc.contributor.author","Lang, Imke"],["dc.contributor.author","Goebel, Cornelia"],["dc.contributor.author","Porzel, Andrea"],["dc.contributor.author","Heilmann, Ingo"],["dc.contributor.author","Feussner, Ivo"],["dc.date.accessioned","2018-11-07T11:17:22Z"],["dc.date.available","2018-11-07T11:17:22Z"],["dc.date.issued","2008"],["dc.description.abstract","The dioxygenation of PUFAs (poly unsaturated fatty acids) in plants is mainly catalysed by members of the LOX (lipoxygenase) enzyme family. LOX products may be further metabolized, and are known as signalling substances in plant development and in responses to wounding and pathogen attack. In contrast with the situation in eukaryotes, information on the relevance of lipid peroxide metabolism in prokaryotic organisms is scarce. Therefore, we aimed to analyse LOXs and oxylipin patterns of cyanobacterial origin. A search of the genomic sequence of the cyanobacterium Nostoc sp. PCC 7120 suggested an open reading frame encoding a putative LOX named NspLOX that harboured an N-terminal extension. Individual analysis of recombinant C-terminal domain revealed enzymatic activity as a linoleate (9R)LOX. Analysis of the full-length NspLOX protein, however, revealed linoleate diol synthase activity, generating (10E,12E)9,14-dihydroxy-10,12-octadecadienoic acid as the main product from LA (linoleic acid) and (10E,12E,14E)-9,16-dihydroxy- 10, 12,14-octadecatrienoic acid as the main product from ALA (alpha-LA) substrates respectively, with ALA as preferred substrate. The enzyme exhibited a broad pH optimum between pH 7 and pH 10. Soluble extracts of Nostoc sp. contain more 9-LOX-derived hydroperoxides in sonified than in non-sonified cells, but products of full-length NspLOX were not detectable under the conditions used. As no other LOX-like sequence was identified in the genome of Nostoc sp. PCC 7120, the results presented suggest that (9R)LOX-derived oxylipins may represent the endogenous products of NspLOX. Based on the biochemical results of NspLOX, we suggest that this bifunctional enzyme may represent a more ancient way to control the intracellular amount of oxylipins in this cyanobacterium."],["dc.identifier.doi","10.1042/BJ20071277"],["dc.identifier.isi","000253618900014"],["dc.identifier.pmid","18031288"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/54788"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Portland Press Ltd"],["dc.relation.issn","0264-6021"],["dc.title","A lipoxygenase with linoleate diol synthase activity from Nostoc sp PCC 7120"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2010Book Chapter [["dc.bibliographiccitation.firstpage","277"],["dc.bibliographiccitation.lastpage","291"],["dc.bibliographiccitation.seriesnr","16"],["dc.contributor.author","Mosblech, Alina"],["dc.contributor.author","Feussner, Ivo"],["dc.contributor.author","Heilmann, Ingo"],["dc.contributor.editor","Munnik, Teun"],["dc.date.accessioned","2018-09-13T06:48:33Z"],["dc.date.available","2018-09-13T06:48:33Z"],["dc.date.issued","2010"],["dc.description.abstract","Oxylipins are derived from the oxidation of polyunsaturated fatty acids. Further conversion of the resulting fatty acid hydroperoxides gives rise to a multitude of oxylipin classes, including hydroxy-, oxo-, or keto fatty acids, volatile aldehydes, and the phytohormone, jasmonic acid (JA). Oxylipins may be structurally further diversified by esterification, i.e., to plastidial glycolipids, Arabidopsides, or conjugation to amino acids. Oxylipin research so far has focused mainly on the investigation of jasmonates and their roles in wound signaling and plant development. In contrast, the physiological roles of other oxylipins are by far less well understood, in part because enzymes responsible for their formation are not well characterized. This chapter aims at giving an overview of plant oxylipin signaling, highlighting recent discoveries of new roles for different oxylipins in the regulation of developmental or adaptational processes."],["dc.identifier.doi","10.1007/978-3-642-03873-0_18"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15699"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.publisher","Springer"],["dc.publisher.place","Berlin, Heidelberg"],["dc.relation.crisseries","Plant Cell Monographs"],["dc.relation.doi","10.1007/978-3-642-03873-0"],["dc.relation.isbn","978-3-642-03872-3"],["dc.relation.isbn","978-3-642-03873-0"],["dc.relation.ispartof","Lipid Signaling in Plants"],["dc.relation.ispartofseries","Plant Cell Monographs; 16"],["dc.title","Oxylipin Signaling and Plant Growth"],["dc.type","book_chapter"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]Details DOI2015Journal Article [["dc.bibliographiccitation.firstpage","764"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Metabolomics"],["dc.bibliographiccitation.lastpage","777"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Kaever, Alexander"],["dc.contributor.author","Landesfeind, Manuel"],["dc.contributor.author","Feussner, Kirstin"],["dc.contributor.author","Mosblech, Alina"],["dc.contributor.author","Heilmann, Ingo"],["dc.contributor.author","Morgenstern, Burkhard"],["dc.contributor.author","Feussner, Ivo"],["dc.contributor.author","Meinicke, Peter"],["dc.date.accessioned","2018-11-07T09:56:52Z"],["dc.date.available","2018-11-07T09:56:52Z"],["dc.date.issued","2015"],["dc.description.abstract","A central aim in the evaluation of non-targeted metabolomics data is the detection of intensity patterns that differ between experimental conditions as well as the identification of the underlying metabolites and their association with metabolic pathways. In this context, the identification of metabolites based on non-targeted mass spectrometry data is a major bottleneck. In many applications, this identification needs to be guided by expert knowledge and interactive tools for exploratory data analysis can significantly support this process. Additionally, the integration of data from other omics platforms, such as DNA microarray-based transcriptomics, can provide valuable hints and thereby facilitate the identification of metabolites via the reconstruction of related metabolic pathways. We here introduce the MarVis-Pathway tool, which allows the user to identify metabolites by annotation of pathways from cross-omics data. The analysis is supported by an extensive framework for pathway enrichment and meta-analysis. The tool allows the mapping of data set features by ID, name, and accurate mass, and can incorporate information from adduct and isotope correction of mass spectrometry data. MarVis-Pathway was integrated in the MarVis-Suite (http://marvis.gobics.de), which features the seamless highly interactive filtering, combination, clustering, and visualization of omics data sets. The functionality of the new software tool is illustrated using combined mass spectrometry and DNA microarray data. This application confirms jasmonate biosynthesis as important metabolic pathway that is upregulated during the wound response of Arabidopsis plants."],["dc.identifier.doi","10.1007/s11306-014-0734-y"],["dc.identifier.isi","000354137100020"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11152"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37052"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","1573-3890"],["dc.relation.issn","1573-3882"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","MarVis-Pathway: integrative and exploratory pathway analysis of non-targeted metabolomics data"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]Details DOI WOS2011Journal Article [["dc.bibliographiccitation.firstpage","841"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","New Phytologist"],["dc.bibliographiccitation.lastpage","854"],["dc.bibliographiccitation.volume","192"],["dc.contributor.author","Ternes, Philipp"],["dc.contributor.author","Feussner, Kirstin"],["dc.contributor.author","Werner, Stephanie"],["dc.contributor.author","Lerche, Jennifer"],["dc.contributor.author","Iven, Tim"],["dc.contributor.author","Heilmann, Ingo"],["dc.contributor.author","Riezman, Howard"],["dc.contributor.author","Feussner, Ivo"],["dc.date.accessioned","2018-11-07T08:49:26Z"],["dc.date.available","2018-11-07T08:49:26Z"],["dc.date.issued","2011"],["dc.description.abstract","The bioactive lipid ceramide is produced by the enzyme ceramide synthase, which exists in several isoforms in most eukaryotic organisms. Here, we investigated functional differences between the three ceramide synthase isoforms in Arabidopsis thaliana. The biochemical properties of the three ceramide synthases were investigated by comparing lipid profiles of yeast strains expressing LOH1, LOH2 or LOH3 with those of wild-type and loh1, loh2 and loh3 knockout plants. Expression profiles of the ceramide synthases and of the pathogenesis-related gene PR-1 were investigated by real-time PCR. Each ceramide synthase isoform showed a characteristic preference regarding acyl-CoA chain length as well as sphingoid base hydroxylation, which matches the pattern of ceramide and glucosylceramide species found in leaves. After extended culture under short-day conditions, loh1 plants showed spontaneous cell death accompanied by enhanced expression of PR-1. The levels of free trihydroxy sphingoid bases as well as ceramide and glucosylceramide species with C(16) fatty acid were significantly elevated while species with C(20)-C(28) fatty acids were reduced. These data suggest that spontaneous cell death in the loh1 line is triggered either by the accumulation of free trihydroxy sphingoid bases or ceramide species with C(16) fatty acid."],["dc.identifier.doi","10.1111/j.1469-8137.2011.03852.x"],["dc.identifier.isi","000297845300010"],["dc.identifier.pmid","21883234"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/21454"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","0028-646X"],["dc.title","Disruption of the ceramide synthase LOH1 causes spontaneous cell death in Arabidopsis thaliana"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS