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Peter Suhrkamp und sein Verlag stehen für den kulturellen Wiederaufbau: Suhrkamp erhält 1945 die erste Verlagslizenz, sein Programm prägt die geistige Identität der jungen Republik. Der Verleger wirkt im Stillen als Katalysator bei der Entstehung von Werken, er gibt Autoren die intellektuelle Heimat, in der entstehen kann, was zur literarischen Signatur Nachkriegsdeutschlands werden wird. Die Frage nach seinem Erfolgsrezept beantwortet Wolfgang Schopf mit einem Blick auf die Schätze des »Archivs der Peter Suhrkamp Stiftung an der Johann Wolfgang Goethe-Universität«.
Es mag generell lohnend sein, bei Fazetien und Schwänken die eingefahrenen Wege von Stoff- und Gattungsgeschichte zu verlassen und analytisch genau zu werden, denn in den Niederungen des ‚niederen’ Erzählens sind komplexe Spuren epistemischer Verunsicherungen zu entdecken. Was indes speziell die Repräsentationen religiöser Praxis in frühmodernen Schwankerzählungen anbelangt, wäre von Fall zu Fall zu urteilen. So sehr Reliquienpraxis im 16. Jahrhundert ins Zentrum konfessioneller Konflikte gerät, so wenig kann das schwankhafte Erzählen von ihr immer schon eindeutig auf die Seite frühmoderner Pluralisierungen geschlagen werden. Solches Erzählen kann vielmehr einerseits als Ort konfessionalistischer Verarbeitung und Eindämmung sozialer, religiöser, ideologischer Differenz genützt werden. Andererseits steht es aber fallweise auch dort als Raum literarischen Probehandelns zur Verfügung, wo es schwer oder unmöglich zu sein scheint, Konkurrenzen relevanter Propositionen, Orientierungskomplexe oder Geltungsfonds durch Negativierung und Asymmetrisierung zu entschärfen. Dann dürfte indes von Pluralisierungen, auch solchen des Religiösen, die Rede sein. Einstweilen offen bliebe hierbei allerdings, ob es sich allein um die Verarbeitungs-, oder auch um Produktionsformen des frühzeitlichen Umbaus der Welt handelt.
The thermolabile triazenides M[tBu3SiNNNSiMetBu2] (M = Li, Na) are accessible from the reaction of tBu2MeSiN3 with the silanides MSitBu3 (M = Li, Na) at −78 °C in THF. At r. t. N2 elimination from the triazenides M[tBu3SiNNNSiMetBu2] (M = Li, Na) takes place with the formation of M[N(SiMetBu2)(SitBu3)] (M = Li, Na). X-Ray quality crystals of Li(THF)[N(SiMetBu2)(SitBu3)] (orthorhombic, Pna21) are obtained from a benzene solution at ambient temperature. In contrast to the structures of the unsolvated silanides MSitBu3 (M = Li, Na), the THF adduct Li(THF)3SitBu3 is monomeric in the solid state (orthorhombic, Pna21).
cGMP- and cAMP-dependent protein kinases (cGK and cAK) mediate the inhibitory effects of endothelium-derived messenger molecules nitric oxide and prostacyclin on platelets. To understand the mechanisms involved in platelet inhibition we searched for new substrates of cGK and cAK. We identified Rap1GAP2, the only GTPase-activating protein of Rap1 in platelets. Rap1 is a guanine-nucleotide binding protein that controls integrin activity, platelet adhesion and aggregation. Rap1GAP2 is required to turn over Rap1-GTP to Rap1-GDP resulting in the inactivation of integrins and reduced cellular adhesion. Using phospho-specific antibodies we demonstrate phosphorylation of endogenous Rap1GAP2 on serine 7 by cGK and cAK in intact platelets. Yeast-two-hybrid screening revealed an interaction of the phosphoserine/-threonine binding adapter protein 14-3-3 with Rap1GAP2, and we mapped the 14-3-3 binding site to the N-terminus of Rap1GAP2 close to the cGK/cAK phosphorylation site. We could show that 14-3-3 binding to Rap1GAP2 requires phosphorylation of serine 9. Platelet activation by ADP and thrombin treatment induces Rap1GAP2 serine 9 phosphorylation and enhances the attachment of 14-3-3 to Rap1GAP2. In contrast, phosphorylation of serine 7 by cGK/cAK leads to the detachment of 14-3-3. Furthermore, Rap1GAP2 serine 7 phosphorylation correlates with the inhibition of Rap1-GTP formation by cGMP and cAMP in platelets. Cell adhesion experiments provide additional evidence that Rap1GAP2 is activated by the detachment of 14-3-3. Point mutants of Rap1GAP2 deficient in 14-3-3 binding inhibit Rap1-mediated cell adhesion significantly stronger than a Rap1GAP2 mutant that binds 14-3-3 constitutively. Our findings define a novel regulatory mechanism that might contribute to both platelet activation and endothelial inhibition of platelet adhesion and aggregation.
The translation eukaryotic elongation factor 1alpha (eEF1A) is a monomeric GTPase involved in protein synthesis. In addition, this protein is thought to participate in other cellular functions such as actin bundling, cell cycle regulation, and apoptosis. Here we show that eEF1A is associated with the alpha2 subunit of the inhibitory glycine receptor in pulldown experiments with rat brain extracts. Moreover, additional proteins involved in translation like ribosomal S6 protein and p70 ribosomal S6 protein kinase as well as ERK1/2 and calcineurin were identified in the same pulldown approaches. Glycine receptor activation in spinal cord neurons cultured for 1 week resulted in an increased phosphorylation of ribosomal S6 protein. Immunocytochemistry showed that eEF1A and ribosomal S6 protein are localized in the soma, dendrites, and at synapses of cultured hippocampal and spinal cord neurons. Consistent with our biochemical data, immunoreactivities of both proteins were partially overlapping with glycine receptor immunoreactivity in cultured spinal cord and hippocampal neurons. After 5 weeks in culture, eEF1A immunoreactivity was redistributed to the cytoskeleton in about 45% of neurons. Interestingly, the degree of redistribution could be increased at earlier stages of in vitro differentiation by inhibition of either the ERK1/2 pathway or glycine receptors and simultaneous N-methyl-D-aspartate receptor activation. Our findings suggest a functional coupling of eEF1A with both inhibitory and excitatory receptors, possibly involving the ERK-signaling pathway.