Ischebeck, Till

[["dc.bibliographiccitation.firstpage","453"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","The Plant Journal"],["dc.bibliographiccitation.lastpage","468"],["dc.bibliographiccitation.volume","65"],["dc.contributor.author","Ischebeck, Till"],["dc.contributor.author","Stenzel, Irene"],["dc.contributor.author","Hempel, Franziska"],["dc.contributor.author","Jin, X. U."],["dc.contributor.author","Mosblech, Alina"],["dc.contributor.author","Heilmann, Ingo"],["dc.date.accessioned","2018-11-07T08:59:38Z"],["dc.date.available","2018-11-07T08:59:38Z"],["dc.date.issued","2011"],["dc.description.abstract","P>The regulation of pollen tube growth by the phospholipid phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P(2)) is not well understood. The Arabidopsis genome encodes two type A phosphatidylinositol-4-phosphate (PI4P) 5-kinases, PIP5K10 and PIP5K11, which are exclusively expressed in pollen and produce PtdIns(4,5)P(2)in vitro. Fluorescence-tagged PIP5K10 and PIP5K11 localized to lateral subapical plasma membrane microdomains in tobacco pollen tubes in a pattern closely resembling the distribution of PtdIns(4,5)P(2,) with the exception of notably weaker association at the extreme apex. Overexpression of PIP5K10 or PIP5K11 in tobacco pollen tubes resulted in severe tip swelling and altered actin fine structure similar to that reported for overexpression of tobacco Nt-Rac5, a monomeric GTPase known to regulate the actin cytoskeleton. Increased sensitivity of Arabidopsis pip5k10 pip5k11 double mutant pollen tubes to Latrunculin B (LatB) further supports a role for type A PI4P 5-kinases in controlling the actin cytoskeleton. Despite the disruption of both its type A PI4P 5-kinases, the pip5k10 pip5k11 double mutant was fertile, indicating that one of the remaining type B PI4P 5-kinase isoforms might be functionally redundant with PIP5K10 and PIP5K11. Antagonistic effects of PIP5K11 and the Nt-Rac5-specific guanine nucleotide dissociation inhibitor, Nt-RhoGDI2, on tip swelling observed in coexpression-titration experiments indicate a link between PtdIns(4,5)P(2) and Rac-signaling in pollen tubes. The data suggest that type A PI4P 5-kinases influence the actin cytoskeleton in pollen tubes in part by counteracting Nt-RhoGDI2, possibly contributing to the control of the pool of plasma membrane-associated Nt-Rac5."],["dc.description.sponsorship","German Research Foundation (DFG) [He3424/1]"],["dc.identifier.doi","10.1111/j.1365-313X.2010.04435.x"],["dc.identifier.isi","000286619000011"],["dc.identifier.pmid","21265898"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/23950"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell Publishing, Inc"],["dc.relation.issn","0960-7412"],["dc.title","Phosphatidylinositol-4,5-bisphosphate influences Nt-Rac5-mediated cell expansion in pollen tubes of Nicotiana tabacum"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","452"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Plants"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Stenzel, Irene"],["dc.contributor.author","Ischebeck, Till"],["dc.contributor.author","Vu-Becker, Linh Hai"],["dc.contributor.author","Riechmann, Mara"],["dc.contributor.author","Krishnamoorthy, Praveen"],["dc.contributor.author","Fratini, Marta"],["dc.contributor.author","Heilmann, Ingo"],["dc.date.accessioned","2021-04-14T08:26:23Z"],["dc.date.available","2021-04-14T08:26:23Z"],["dc.date.issued","2020"],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft"],["dc.identifier.doi","10.3390/plants9040452"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81922"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.publisher","MDPI"],["dc.relation.eissn","2223-7747"],["dc.rights","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Coordinated Localization and Antagonistic Function of NtPLC3 and PI4P 5-Kinases in the Subapical Plasma Membrane of Tobacco Pollen Tubes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","13"],["dc.bibliographiccitation.issue","1-4"],["dc.bibliographiccitation.journal","PROTOPLASMA"],["dc.bibliographiccitation.lastpage","31"],["dc.bibliographiccitation.volume","240"],["dc.contributor.author","Ischebeck, Till"],["dc.contributor.author","Seiler, Stephan"],["dc.contributor.author","Heilmann, Ingo"],["dc.date.accessioned","2018-11-07T08:44:51Z"],["dc.date.available","2018-11-07T08:44:51Z"],["dc.date.issued","2010"],["dc.description.abstract","Phosphoinositides (PIs) are minor, but essential phospholipid constituents of eukaryotic membranes, and are involved in the regulation of various physiological processes. Recent genetic and cell biological advances indicate that PIs play important roles in the control of polar tip growth in plant cells. In root hairs and pollen tubes, PIs control directional membrane trafficking required for the delivery of cell wall material and membrane area to the growing tip. So far, the exact mechanisms by which PIs control polarity and tip growth are unresolved. However, data gained from the analysis of plant, fungal and animal systems implicate PIs in the control of cytoskeletal dynamics, ion channel activity as well as vesicle trafficking. The present review aims at giving an overview of PI roles in eukaryotic cells with a special focus on functions pertaining to the control of cell polarity. Comparative screening of plant and fungal genomes suggests diversification of the PI system with increasing organismic complexity. The evolutionary conservation of the PI system among eukaryotic cells suggests a role for PIs in tip growing cells in models where PIs so far have not been a focus of attention, such as fungal hyphae."],["dc.identifier.doi","10.1007/s00709-009-0093-0"],["dc.identifier.isi","000275750200003"],["dc.identifier.pmid","20091065"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/4183"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/20290"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","Wien"],["dc.relation.issn","0033-183X"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","At the poles across kingdoms: phosphoinositides and polar tip growth"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["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"]]

[["dc.bibliographiccitation.firstpage","3312"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","The Plant Cell"],["dc.bibliographiccitation.lastpage","3330"],["dc.bibliographiccitation.volume","20"],["dc.contributor.author","Ischebeck, Till"],["dc.contributor.author","Stenzel, Irene"],["dc.contributor.author","Heilmann, Ingo"],["dc.date.accessioned","2018-11-07T11:08:50Z"],["dc.date.available","2018-11-07T11:08:50Z"],["dc.date.issued","2008"],["dc.description.abstract","Phosphatidylinositol-4,5-bisphosphate [PtdIns(4,5)P(2)] occurs in the apical plasma membrane of growing pollen tubes. Because enzymes responsible for PtdIns(4,5) P(2) production at that location are uncharacterized, functions of PtdIns( 4,5) P(2) in pollen tube tip growth are unresolved. Two candidate genes encoding pollen-expressed Arabidopsis thaliana phosphatidylinositol-4-phosphate 5-kinases (PI4P 5-kinases) of Arabidopsis subfamily B were identified (PIP5K4 and PIP5K5), and their recombinant proteins were characterized as being PI4P 5-kinases. Pollen of T-DNA insertion lines deficient in both PIP5K4 and PIP5K5 exhibited reduced pollen germination and defects in pollen tube elongation. Fluorescence-tagged PIP5K4 and PIP5K5 localized to an apical plasma membrane microdomain in Arabidopsis and tobacco (Nicotiana tabacum) pollen tubes, and overexpression of either PIP5K4 or PIP5K5 triggered multiple tip branching events. Further studies using the tobacco system revealed that overexpression caused massive apical pectin deposition accompanied by plasma membrane invaginations. By contrast, callose deposition and cytoskeletal structures were unaltered in the overexpressors. Morphological effects depended on PtdIns(4,5) P(2) production, as an inactive enzyme variant did not produce any effects. The data indicate that excessive PtdIns(4,5) P2 production by type B PI4P 5-kinases disturbs the balance of membrane trafficking and apical pectin deposition. Polar tip growth of pollen tubes may thus be modulated by PtdIns(4,5) P(2) via regulatory effects on membrane trafficking and/or apical pectin deposition."],["dc.description.sponsorship","German Research Foundation"],["dc.identifier.doi","10.1105/tpc.108.059568"],["dc.identifier.isi","000262861700015"],["dc.identifier.pmid","19060112"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/52881"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Plant Biologists"],["dc.relation.issn","1040-4651"],["dc.title","Type B Phosphatidylinositol-4-Phosphate 5-Kinases Mediate Arabidopsis and Nicotiana tabacum Pollen Tube Growth by Regulating Apical Pectin Secretion"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1475"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Current Biology"],["dc.bibliographiccitation.lastpage","1482"],["dc.bibliographiccitation.volume","25"],["dc.contributor.author","Steinhorst, Leonie"],["dc.contributor.author","Maehs, Anette"],["dc.contributor.author","Ischebeck, Till"],["dc.contributor.author","Zhang, C."],["dc.contributor.author","Zhang, Xinxin"],["dc.contributor.author","Arendt, Sibylle"],["dc.contributor.author","Schueltke, Stefanie"],["dc.contributor.author","Heilmann, Ingo"],["dc.contributor.author","Kudla, Joerg"],["dc.date.accessioned","2018-11-07T09:56:35Z"],["dc.date.available","2018-11-07T09:56:35Z"],["dc.date.issued","2015"],["dc.description.abstract","Polarized tip growth is a fundamental process of specialized eukaryotic cells like neuronal axons, fungal hyphae, and plant root hairs and pollen tubes. In pollen tubes, a tip-focused oscillating Ca2+ gradient governs ions fluxes, vesicle transport, and cytoskeleton dynamics to ensure proper polarized cell growth [1, 2]. While a crucial role of vacuolar Ca2+ signaling is established for cellular movements like guard cell dynamics [3-5], its contribution to polarized growth remains to be defined. Here we identified the two closely related tonoplast-localized Ca2+-sensor proteins CBL2 and CBL3 as crucial regulators of vacuolar dynamics and polarized pollen tube growth. Overexpression of CBL2 or CBL3 in Arabidopsis and tobacco pollen tubes affected vacuolar morphology, pollen germination, and tube growth, but did not alter actin organization, PI(4,5)P-2 distribution, or tip-focused Ca2+ oscillations. Similarly, loss of function of each single Ca2+ sensor and cbl2/cbl3 double mutants exhibited impaired pollen tube growth in vitro and in vivo. Both Ca2+ sensors interacted with the kinase CIPK12, which translocated from the cytoplasm to the vacuolar membrane upon this interaction. Also, overexpression of CIPK12 induced severe vacuolar phenotypes, and loss of function of CIPK12 lead to impairment of polar growth. Remarkably, co-expression of CBL2 or CBL3 with CIPK12 resulted in a phosphorylation-dependent, massively enhanced vacuolar inflation and further disruption of polar growth. Together, these findings identify an essential role of the vacuole and vacuolar Ca2+ signaling for polarized tip growth. We propose that a faithfully balanced activity of Ca2+-activated CBL2/3-CIPK12 complexes fulfills fundamental functions to enable the fast growth of pollen tubes in higher plants."],["dc.description.sponsorship","DFG [SFB 629, FOR 964]"],["dc.identifier.doi","10.1016/j.cub.2015.03.053"],["dc.identifier.isi","000355556600022"],["dc.identifier.pmid","25936548"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36987"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.relation.issn","1879-0445"],["dc.relation.issn","0960-9822"],["dc.title","Vacuolar CBL-CIPK12 Ca2+-Sensor-Kinase Complexes Are Required for Polarized Pollen Tube Growth"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","387"],["dc.bibliographiccitation.journal","Biochemical Journal"],["dc.bibliographiccitation.lastpage","399"],["dc.bibliographiccitation.volume","415"],["dc.contributor.author","Koenig, Sabine"],["dc.contributor.author","Ischebeck, Till"],["dc.contributor.author","Lerche, Jennifer"],["dc.contributor.author","Stenzel, Irene"],["dc.contributor.author","Heilmann, Ingo"],["dc.date.accessioned","2018-11-07T11:09:18Z"],["dc.date.available","2018-11-07T11:09:18Z"],["dc.date.issued","2008"],["dc.description.abstract","Plants exposed to hyperosmotic stress undergo changes in membrane dynamics and lipid composition to maintain cellular integrity and avoid membrane leakage. Various plant species respond to hyperosmotic stress with transient increases in PtdIns(4,5)P-2; however, the physiological role of such increases is unresolved. The plasma membrane represents the outermost barrier between the symplast of plant cells and its apoplastic surroundings. In the present Study, the spatio-temporal dynamics of stress-induced changes in phosphoinositides were analysed in subcellular fractions of Arabidopsis leaves to delineate possible physiological roles. Unlabelled lipids were separated by TLC and quantified by gas-chromatographic detection of associated fatty acids. Transient PtdIns(4,5)P-2 increases upon exposure to hyperosmotic stress were detected first in enriched plasmamembrane fractions, however, at later time points, PtdIns(4,5)P-2 was increased in the endomembrane fractions of the corresponding two-phase systems. When major endomembranes were enriched from rosette leaves prior to hyperosmotic stress and during stimulation for 60 min, no stress-induced increases in the levels of PtdIns(4,5)P-2 were found in fractions enriched for endoplasmic reticulum, nuclei or plastidial membranes. Instead, increased PtdIns(4,5)P-2 was found in CCVs (clathrin-coated vesicles), which proliferated several-fold in mass within 60 min of hyperosmotic stress, according to the abundance of CCV-associated proteins and lipids. Monitoring the subcellular distribution of fluorescence-tagged reporters for clathrin and PtdIns(4,5)P-2 during transient co-expression in onion epidermal cells indicates rapid stress-induced co-localization of clathrin with PtdIns(4,5)P-2 at the plasma membrane. The results indicate that PtdIns(4,5)P-2 may act in stress-induced formation of CCVs in plant cells, highlighting the evolutionary conservation of the phosphoinositide system between organismic kingdoms."],["dc.description.sponsorship","German Research Foundation [DFG (Deutsche Forschungsgemeinschaft)]"],["dc.identifier.doi","10.1042/BJ20081306"],["dc.identifier.isi","000260649700006"],["dc.identifier.pmid","18721128"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/5701"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/52975"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Portland Press Ltd"],["dc.relation.issn","1470-8728"],["dc.relation.issn","0264-6021"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Salt-stress-induced association of phosphatidylinositol 4,5-bisphosphate with clathrin-coated vesicles in plants"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","submitted_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e51454"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Maehs, Anette"],["dc.contributor.author","Ischebeck, Till"],["dc.contributor.author","Heilig, Yvonne"],["dc.contributor.author","Stenzel, Irene"],["dc.contributor.author","Hempel, Franziska"],["dc.contributor.author","Seiler, Stephan"],["dc.contributor.author","Heilmann, Ingo"],["dc.date.accessioned","2018-11-07T09:02:18Z"],["dc.date.available","2018-11-07T09:02:18Z"],["dc.date.issued","2012"],["dc.description.abstract","Fungal hyphae and plant pollen tubes are among the most highly polarized cells known and pose extraordinary requirements on their cell polarity machinery. Cellular morphogenesis is driven through the phospholipid-dependent organization at the apical plasma membrane. We characterized the contribution of phosphoinositides (PIs) in hyphal growth of the filamentous ascomycete Neurospora crassa. MSS-4 is an essential gene and its deletion resulted in spherically growing cells that ultimately lyse. Two conditional mss-4-mutants exhibited altered hyphal morphology and aberrant branching at restrictive conditions that were complemented by expression of wild type MSS-4. Recombinant MSS-4 was characterized as a phosphatidylinositolmonophosphate-kinase phosphorylating phosphatidylinositol 4-phosphate (PtdIns4P) to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P-2). PtdIns3P was also used as a substrate. Sequencing of two conditional mss-4 alleles identified a single substitution of a highly conserved Y750 to N. The biochemical characterization of recombinant protein variants revealed Y750 as critical for PI4P 5-kinase activity of MSS-4 and of plant PI4P 5-kinases. The conditional growth defects of mss-4 mutants were caused by severely reduced activity of MSS-4(Y750N), enabling the formation of only trace amounts of PtdIns(4,5)P-2. In N. crassa hyphae, PtdIns(4,5)P-2 localized predominantly in the plasma membrane of hyphae and along septa. Fluorescence-tagged MSS-4 formed a subapical collar at hyphal tips, localized to constricting septa and accumulated at contact points of fusing N. crassa germlings, indicating MSS-4 is responsible for the formation of relevant pools of PtdIns(4,5)P-2 that control polar and directional growth and septation. N. crassa MSS-4 differs from yeast, plant and mammalian PI4P 5-kinases by containing additional protein domains. The N-terminal domain of N. crassa MSS-4 was required for correct membrane association. The data presented for N. crassa MSS-4 and its roles in hyphal growth are discussed with a comparative perspective on PI-control of polar tip growth in different organismic kingdoms."],["dc.identifier.doi","10.1371/journal.pone.0051454"],["dc.identifier.isi","000312386600026"],["dc.identifier.pmid","23272106"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8449"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/24652"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Public Library Science"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.title","The Essential Phosphoinositide Kinase MSS-4 Is Required for Polar Hyphal Morphogenesis, Localizing to Sites of Growth and Cell Fusion in Neurospora crassa"],["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"]]

[["dc.bibliographiccitation.firstpage","124"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","The Plant Cell"],["dc.bibliographiccitation.lastpage","141"],["dc.bibliographiccitation.volume","20"],["dc.contributor.author","Stenzel, Irene"],["dc.contributor.author","Ischebeck, Till"],["dc.contributor.author","Koenig, Sabine"],["dc.contributor.author","Holubowska, Anna"],["dc.contributor.author","Sporysz, Marta"],["dc.contributor.author","Hause, Bettina"],["dc.contributor.author","Heilmann, Ingo"],["dc.date.accessioned","2018-11-07T11:20:40Z"],["dc.date.available","2018-11-07T11:20:40Z"],["dc.date.issued","2008"],["dc.description.abstract","Root hairs are extensions of root epidermal cells and a model system for directional tip growth of plant cells. A previously uncharacterized Arabidopsis thaliana phosphatidylinositol-4-phosphate 5-kinase gene (PIP5K3) was identified and found to be expressed in the root cortex, epidermal cells, and root hairs. Recombinant PIP5K3 protein was catalytically active and converted phosphatidylinositol-4-phosphate to phosphatidylinositol-4,5-bisphosphate [PtdIns(4,5)P(2)]. Arabidopsis mutant plants homozygous for T-DNA-disrupted PIP5K3 alleles were compromised in root hair formation, a phenotype complemented by expression of wild-type PIP5K3 cDNA under the control of a 1500-bp PIP5K3 promoter fragment. Root hair-specific PIP5K3 overexpression resulted in root hair deformation and loss of cell polarity with increasing accumulation of PIP5K3 transcript. Using reestablishment of root hair formation in T-DNA mutants as a bioassay for physiological functionality of engineered PIP5K3 variants, catalytic activity was found to be essential for physiological function, indicating that PtdIns(4,5)P(2) formation is required for root hair development. An N-terminal domain containing membrane occupation and recognition nexus repeats, which is not required for catalytic activity, was found to be essential for the establishment of root hair growth. Fluorescence-tagged PIP5K3 localized to the periphery of the apical region of root hair cells, possibly associating with the plasma membrane and/or exocytotic vesicles. Transient heterologous expression of full-length PIP5K3 in tobacco (Nicotiana tabacum) pollen tubes increased plasma membrane association of a PtdIns(4,5)P(2)-specific reporter in these tip-growing cells. The data demonstrate that root hair development requires PIP5K3-dependent PtdIns(4,5)P(2) production in the apical region of root hair cells."],["dc.identifier.doi","10.1105/tpc.107.052852"],["dc.identifier.isi","000256414400011"],["dc.identifier.pmid","18178770"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/55594"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Plant Biologists"],["dc.relation.issn","1040-4651"],["dc.title","The type B phosphatidylinositol-4-phosphate 5-kinase 3 is essential for root hair formation in Arabidopsis thaliana"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3"],["dc.bibliographiccitation.issue","1-2"],["dc.bibliographiccitation.journal","Plant Reproduction"],["dc.bibliographiccitation.lastpage","20"],["dc.bibliographiccitation.volume","29"],["dc.contributor.author","Heilmann, Ingo"],["dc.contributor.author","Ischebeck, Till"],["dc.date.accessioned","2018-11-07T10:13:19Z"],["dc.date.available","2018-11-07T10:13:19Z"],["dc.date.issued","2016"],["dc.description.abstract","In angiosperms, sexual reproduction is a series of complex biological events that facilitate the distribution of male generative cells for double fertilization. Angiosperms have no motile gametes, and the distribution units of generative cells are pollen grains, passively mobile desiccated structures, capable of delivering genetic material to compatible flowers over long distances and in an adverse environment. The development of pollen (male gametogenesis) and the formation of a pollen tube after a pollen grain has reached a compatible flower (pollen tube growth) are important aspects of plant developmental biology. In recent years, a wealth of information has been gathered about the molecular control of cell polarity, membrane trafficking and cytoskeletal dynamics underlying these developmental processes. In particular, it has been found that regulatory membrane phospholipids, such as phosphoinositides (PIs), are critical regulatory players, controlling key steps of trafficking and polarization. Characteristic features of PIs are the inositol phosphate headgroups of the lipids, which protrude from the cytosolic surfaces of membranes, enabling specific binding and recruitment of numerous protein partners containing specific PI-binding domains. Such recruitment is globally an early event in polarization processes of eukaryotic cells and also of key importance to pollen development and tube growth. Additionally, PIs serve as precursors of other signaling factors with importance to male gametogenesis. This review highlights the recent advances about the roles of PIs in pollen development and pollen function."],["dc.identifier.doi","10.1007/s00497-015-0270-6"],["dc.identifier.isi","000378731200002"],["dc.identifier.pmid","26676144"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/40412"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","2194-7961"],["dc.relation.issn","2194-7953"],["dc.title","Male functions and malfunctions: the impact of phosphoinositides on pollen development and pollen tube growth"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]