Democracy and (the essential content of) fundamental rights: marching in line or precarious balancing act?

This article addresses the question of how democracy and fundamental rights interplay, and compares German and South African law for this purpose. The author argues that democracy requires and presupposes fundamental rights, but that these two values do not always align, and then deals with the question of how to reconcile democracy and fundamental rights in case of conflict. The potential conflict between the two values is sometimes reflected in the relationship between Parliaments as the embodiment of democracy and the Constitutional Courts as the embodiments of fundamental rights (the so- called “counter-majoritarian dilemma”). However, the author rejects the recent critique by some scholars that the German Federal Constitutional Court structurally exceeds its powers vis-à-vis the German Parliament and that there is a permanent judicial overreach. On the contrary, the author argues that Constitutional Courts do not have sufficient tools to counter a democratic backsliding, i.e. the incremental erosion of democracy. Since the author considers democratic backsliding to be a greater and more acute threat to democracy than judicial overreach, he presents the view that the guarantee of the essential content of a right delineates the minimum of a fundamental right in a democratic society. This view is explained using freedom of expression as example

Das Republikprinzip

Seit einiger Zeit kann man in der Presse von Verhandlungen über die Übertragung von Vermögenswerten zwischen Vertretern der Bundesrepublik Deutschland und des Landes Brandenburg einerseits mit Erben des letzten deutschen Kaisers andererseits lesen. Anscheinend geht es nicht nur um erhebliche finanzielle Werte, sondern auch um Geschichtsschreibung und familiäre Selbstdarstellung. Das muss in einer republikanischen Demokratie irritieren. Anlass genug, die Verfassung zu ihrem republikanischen Gehalt zu befragen

Klausur im Öffentlichen Recht für Anfänger: Kein BAföG nach Bologna?

Die Klausur wurde im Herbst-Winter-Semester 2019/20 im Rahmen der Übung im Öffentlichen Recht für Anfänger gestellt (Bearbeitungszeit: 180 Minuten)

Cell–substrate adhesion drives Scar/WAVE activation and phosphorylation by a Ste20-family kinase, which controls pseudopod lifetime

The Scar/WAVE complex is the principal catalyst of pseudopod and lamellipod formation. Here we show that Scar/WAVE’s proline-rich domain is polyphosphorylated after the complex is activated. Blocking Scar/WAVE activation stops phosphorylation in both Dictyostelium and mammalian cells, implying that phosphorylation modulates pseudopods after they have been formed, rather than controlling whether they are initiated. Unexpectedly, phosphorylation is not promoted by chemotactic signaling but is greatly stimulated by cell:substrate adhesion and diminished when cells deadhere. Phosphorylation-deficient or phosphomimetic Scar/WAVE mutants are both normally functional and rescue the phenotype of knockout cells, demonstrating that phosphorylation is dispensable for activation and actin regulation. However, pseudopods and patches of phosphorylation-deficient Scar/WAVE last substantially longer in mutants, altering the dynamics and size of pseudopods and lamellipods and thus changing migration speed. Scar/WAVE phosphorylation does not require ERK2 in Dictyostelium or mammalian cells. However, the MAPKKK homologue SepA contributes substantially—sepA mutants have less steady-state phosphorylation, which does not increase in response to adhesion. The mutants also behave similarly to cells expressing phosphorylation-deficient Scar, with longer-lived pseudopods and patches of Scar recruitment. We conclude that pseudopod engagement with substratum is more important than extracellular signals at regulating Scar/WAVE’s activity and that phosphorylation acts as a pseudopod timer by promoting Scar/WAVE turnover

Lamellipodin tunes cell migration by stabilizing protrusions and promoting adhesion formation

Efficient migration on adhesive surfaces involves the protrusion of lamellipodial actin networks and their subsequent stabilization by nascent adhesions. The actin-binding protein lamellipodin (Lpd) is thought to play a critical role in lamellipodium protrusion, by delivering Ena/VASP proteins onto the growing plus ends of actin filaments and by interacting with the WAVE regulatory complex, an activator of the Arp2/3 complex, at the leading edge. Using B16-F1 melanoma cell lines, we demonstrate that genetic ablation of Lpd compromises protrusion efficiency and coincident cell migration without altering essential parameters of lamellipodia, including their maximal rate of forward advancement and actin polymerization. We also confirmed lamellipodia and migration phenotypes with CRISPR/Cas9-mediated Lpd knockout Rat2 fibroblasts, excluding cell type-specific effects. Moreover, computer-aided analysis of cell-edge morphodynamics on B16-F1 cell lamellipodia revealed that loss of Lpd correlates with reduced temporal protrusion maintenance as a prerequisite of nascent adhesion formation. We conclude that Lpd optimizes protrusion and nascent adhesion formation by counteracting frequent, chaotic retraction and membrane ruffling.This article has an associated First Person interview with the first author of the paper

Loss of Ena/VASP interferes with lamellipodium architecture, motility and integrin-dependent adhesion

Cell migration entails networks and bundles of actin filaments termed lamellipodia and microspikes or filopodia, respectively, as well as focal adhesions, all of which recruit Ena/VASP family members hitherto thought to antagonize efficient cell motility. However, we find these proteins to act as positive regulators of migration in different murine cell lines. CRISPR/Cas9-mediated loss of Ena/VASP proteins reduced lamellipodial actin assembly and perturbed lamellipodial architecture, as evidenced by changed network geometry as well as reduction of filament length and number that was accompanied by abnormal Arp2/3 complex and heterodimeric capping protein accumulation. Loss of Ena/VASP function also abolished the formation of microspikes normally embedded in lamellipodia, but not of filopodia capable of emanating without lamellipodia. Ena/VASP-deficiency also impaired integrin-mediated adhesion accompanied by reduced traction forces exerted through these structures. Our data thus uncover novel Ena/VASP functions of these actin polymerases that are fully consistent with their promotion of cell migration