@article{MahlowHejaziKuhnertetal.2014,
  author    = {Mahlow, Sebastian and Hejazi, Mahdi and Kuhnert, Franziska and Garz, Andreas and Brust, Henrike and Baumann, Otto and Fettke, J{\"o}rg},
  title     = {Phosphorylation of transitory starch by -glucan, water dikinase during starch turnover affects the surface properties and morphology of starch granules},
  series = {New phytologist : international journal of plant science},
  volume    = {203},
  journal   = {New phytologist : international journal of plant science},
  number    = {2},
  publisher = {Wiley-Blackwell},
  address   = {Hoboken},
  issn      = {0028-646X},
  doi       = {10.1111/nph.12801},
  pages     = {495 -- 507},
  year      = {2014},
  abstract  = {Glucan, water dikinase (GWD) is a key enzyme of starch metabolism but the physico-chemical properties of starches isolated from GWD-deficient plants and their implications for starch metabolism have so far not been described. Transgenic Arabidopsis thaliana plants with reduced or no GWD activity were used to investigate the properties of starch granules. In addition, using various in vitro assays, the action of recombinant GWD, -amylase, isoamylase and starch synthase 1 on the surface of native starch granules was analysed. The internal structure of granules isolated from GWD mutant plants is unaffected, as thermal stability, allomorph, chain length distribution and density of starch granules were similar to wild-type. However, short glucan chain residues located at the granule surface dominate in starches of transgenic plants and impede GWD activity. A similarly reduced rate of phosphorylation by GWD was also observed in potato tuber starch fractions that differ in the proportion of accessible glucan chain residues at the granule surface. A model is proposed to explain the characteristic morphology of starch granules observed in GWD transgenic plants. The model postulates that the occupancy rate of single glucan chains at the granule surface limits accessibility to starch-related enzymes.},
  language  = {en}
}
@article{GuljamowDelissenBaumannetal.2012,
  author    = {Guljamow, Arthur and Delissen, Friedmar and Baumann, Otto and Thuenemann, Andreas F. and Dittmann-Th{\"u}nemann, Elke},
  title     = {Unique properties of eukaryote-type actin and profilin horizontally transferred to cyanobacteria},
  series = {PLoS one},
  volume    = {7},
  journal   = {PLoS one},
  number    = {1},
  publisher = {PLoS},
  address   = {San Fransisco},
  issn      = {1932-6203},
  doi       = {10.1371/journal.pone.0029926},
  pages     = {221 -- 231},
  year      = {2012},
  abstract  = {A eukaryote-type actin and its binding protein profilin encoded on a genomic island in the cyanobacterium Microcystis aeruginosa PCC 7806 co-localize to form a hollow, spherical enclosure occupying a considerable intracellular space as shown by in vivo fluorescence microscopy. Biochemical and biophysical characterization reveals key differences between these proteins and their eukaryotic homologs. Small-angle X-ray scattering shows that the actin assembles into elongated, filamentous polymers which can be visualized microscopically with fluorescent phalloidin. Whereas rabbit actin forms thin cylindrical filaments about 100 mu m in length, cyanobacterial actin polymers resemble a ribbon, arrest polymerization at 510 lam and tend to form irregular multi-strand assemblies. While eukaryotic profilin is a specific actin monomer binding protein, cyanobacterial profilin shows the unprecedented property of decorating actin filaments. Electron micrographs show that cyanobacterial profilin stimulates actin filament bundling and stabilizes their lateral alignment into heteropolymeric sheets from which the observed hollow enclosure may be formed. We hypothesize that adaptation to the confined space of a bacterial cell devoid of binding proteins usually regulating actin polymerization in eukaryotes has driven the co-evolution of cyanobacterial actin and profilin, giving rise to an intracellular entity.},
  language  = {en}
}
@article{RichterRolkeBlenauetal.2016,
  author    = {Richter, Katharina Natalia and Rolke, Daniel and Blenau, Wolfgang and Baumann, Otto},
  title     = {Secretory cells in honeybee hypopharyngeal gland: polarized organization and age-dependent dynamics of plasma membrane},
  series = {Cell \& tissue research},
  volume    = {366},
  journal   = {Cell \& tissue research},
  publisher = {Springer},
  address   = {New York},
  issn      = {0302-766X},
  doi       = {10.1007/s00441-016-2423-9},
  pages     = {163 -- 174},
  year      = {2016},
  abstract  = {The honeybee hypopharyngeal gland consists in numerous units, each comprising a secretory cell and a canal cell. The secretory cell discharges its products into a convoluted tubular membrane system, the canaliculus, which is surrounded at regular intervals by rings of actin filaments. Using probes for various membrane components, we analyze the organization of the secretory cells relative to the apicobasal configuration of epithelial cells. The canaliculus was defined by labeling with an antibody against phosphorylated ezrin/radixin/moesin (pERM), a marker protein for the apical membrane domain of epithelial cells. Anti-phosphotyrosine visualizes the canalicular system, possibly by staining the microvillar tips. The open end of the canaliculus leads to a region in which the secretory cell is attached to the canal cell by adherens and septate junctions. The remaining plasma membrane stains for Na,K-ATPase and spectrin and represents the basolateral domain. We also used fluorophore-tagged phalloidin, anti-phosphotyrosine and anti-pERM as probes for the canaliculus in order to describe fine-structural changes in the organization of the canalicular system during the adult life cycle. These probes in conjunction with fluorescence microscopy allow the fast and detailed three-dimensional analysis of the canalicular membrane system and its structural changes in a developmental mode or in response to environmental factors.},
  language  = {en}
}
@article{KloseRolkeBaumann2017,
  author    = {Klose, Sascha Peter and Rolke, Daniel and Baumann, Otto},
  title     = {Morphogenesis of honeybee hypopharyngeal gland during pupal development},
  series = {Frontiers in zoology},
  volume    = {14},
  journal   = {Frontiers in zoology},
  publisher = {BioMed Central},
  address   = {London},
  issn      = {1742-9994},
  doi       = {10.1186/s12983-017-0207-z},
  year      = {2017},
  abstract  = {Background The hypopharyngeal gland of worker bees contributes to the production of the royal jelly fed to queens and larvae. The gland consists of thousands of two-cell units that are composed of a secretory cell and a duct cell and that are arranged in sets of about 12 around a long collecting duct. Results By fluorescent staining, we have examined the morphogenesis of the hypopharyngeal gland during pupal life, from a saccule lined by a pseudostratified epithelium to the elaborate organ of adult worker bees. The hypopharyngeal gland develops as follows. (1) Cell proliferation occurs during the first day of pupal life in the hypopharyngeal gland primordium. (2) Subsequently, the epithelium becomes organized into rosette-like units of three cells. Two of these will become the secretory cell and the duct cell of the adult secretory units; the third cell contributes only temporarily to the development of the secretory units and is eliminated by apoptosis in the second half of pupal life. (3) The three-cell units of flask-shaped cells undergo complex changes in cell morphology. Thus, by mid-pupal stage, the gland is structurally similar to the adult hypopharyngeal gland. (4) Concomitantly, the prospective secretory cell attains its characteristic subcellular organization by the invagination of a small patch of apical membrane domain, its extension to a tube of about 100 μm in length (termed a canaliculus), and the expansion of the tube to a diameter of about 3 μm. (6) Finally, the canaliculus-associated F-actin system becomes reorganized into rings of bundled actin filaments that are positioned at regular distances along the membrane tube. Conclusions The morphogenesis of the secretory units in the hypopharyngeal gland of the worker bee seems to be based on a developmental program that is conserved, with slight modification, among insects for the production of dermal glands. Elaboration of the secretory cell as a unicellular seamless epithelial tube occurs by invagination of the apical membrane, its extension likely by targeted exocytosis and its expansion, and finally the reorganisation of the membrane-associated F-actin system. Our work is fundamental for future studies of environmental effects on hypopharyngeal gland morphology and development.},
  language  = {en}
}
@misc{KloseRolkeBaumann2017,
  author    = {Klose, Sascha Peter and Rolke, Daniel and Baumann, Otto},
  title     = {Morphogenesis of honeybee hypopharyngeal gland during pupal development},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-395712},
  pages     = {14},
  year      = {2017},
  abstract  = {Background The hypopharyngeal gland of worker bees contributes to the production of the royal jelly fed to queens and larvae. The gland consists of thousands of two-cell units that are composed of a secretory cell and a duct cell and that are arranged in sets of about 12 around a long collecting duct. Results By fluorescent staining, we have examined the morphogenesis of the hypopharyngeal gland during pupal life, from a saccule lined by a pseudostratified epithelium to the elaborate organ of adult worker bees. The hypopharyngeal gland develops as follows. (1) Cell proliferation occurs during the first day of pupal life in the hypopharyngeal gland primordium. (2) Subsequently, the epithelium becomes organized into rosette-like units of three cells. Two of these will become the secretory cell and the duct cell of the adult secretory units; the third cell contributes only temporarily to the development of the secretory units and is eliminated by apoptosis in the second half of pupal life. (3) The three-cell units of flask-shaped cells undergo complex changes in cell morphology. Thus, by mid-pupal stage, the gland is structurally similar to the adult hypopharyngeal gland. (4) Concomitantly, the prospective secretory cell attains its characteristic subcellular organization by the invagination of a small patch of apical membrane domain, its extension to a tube of about 100 μm in length (termed a canaliculus), and the expansion of the tube to a diameter of about 3 μm. (6) Finally, the canaliculus-associated F-actin system becomes reorganized into rings of bundled actin filaments that are positioned at regular distances along the membrane tube. Conclusions The morphogenesis of the secretory units in the hypopharyngeal gland of the worker bee seems to be based on a developmental program that is conserved, with slight modification, among insects for the production of dermal glands. Elaboration of the secretory cell as a unicellular seamless epithelial tube occurs by invagination of the apical membrane, its extension likely by targeted exocytosis and its expansion, and finally the reorganisation of the membrane-associated F-actin system. Our work is fundamental for future studies of environmental effects on hypopharyngeal gland morphology and development.},
  language  = {en}
}
@article{Baumann2001,
  author    = {Baumann, Otto},
  title     = {Disruption of actin filaments causes redistribution of ryanodine receptor Ca2+ channels in honeybee photoreceptor cells},
  year      = {2001},
  language  = {en}
}
@article{Baumann2001,
  author    = {Baumann, Otto},
  title     = {Distribution of nonmuscle myosin-II in honeybee photoreceptor cells and its possible role in maintaining compound eye architecture},
  year      = {2001},
  language  = {en}
}
@article{BaumannWalz2001,
  author    = {Baumann, Otto and Walz, Bernd},
  title     = {The endoplasmic reticulum of animal cells and its organization into structural and functional domains},
  year      = {2001},
  language  = {en}
}
@article{Baumann2001,
  author    = {Baumann, Otto},
  title     = {Posterior midgut epithelial cells differ in their organization of the membrane skeleton from other Drosophila epithelia},
  year      = {2001},
  language  = {en}
}
@article{DubreuilGrushkoBaumann2001,
  author    = {Dubreuil, R. R. and Grushko, T. and Baumann, Otto},
  title     = {Differential effects of a labial mutation on the development, structure, and function of stomach acid-secreting cells in Drosophila larvae and adults},
  year      = {2001},
  language  = {en}
}