Weak Poisson structures on infinite dimensional manifolds and hamiltonian actions

We introduce a notion of a weak Poisson structure on a manifold $M$ modeled on a locally convex space. This is done by specifying a Poisson bracket on a subalgebra \cA \subeq C^\infty(M) which has to satisfy a non-degeneracy condition (the differentials of elements of \cA separate tangent vectors) and we postulate the existence of smooth Hamiltonian vector fields. Motivated by applications to Hamiltonian actions, we focus on affine Poisson spaces which include in particular the linear and affine Poisson structures on duals of locally convex Lie algebras. As an interesting byproduct of our approach, we can associate to an invariant symmetric bilinear form $\kappa$ on a Lie algebra \g and a $\kappa$-skew-symmetric derivation $D$ a weak affine Poisson structure on \g itself. This leads naturally to a concept of a Hamiltonian $G$-action on a weak Poisson manifold with a \g-valued momentum map and hence to a generalization of quasi-hamiltonian group actions

The Relationship between Physical Growth and Infant Behavioral Development in Rural Guatemala

The present study investigated the relationship between a number of anthropometric indices and behavioral development during the first 2 years of life in rural Guatemala. Length and weight were the indices most strongly correlated with behavioral development. If the effect of the infant\u27s length and weight was statistically controlled for, none of the other anthropometric variables explained a significant proportion of the variance in behavioral development. Con- trolling for length (or weight) assessed at the same age as the behavioral assessment, length (or weight) for younger ages was not significantly correlated with behavioral development. Changes in length or weight over time were correlated with changes in behavioral performance. We were unable to explain the association between physical growth and behavioral development by a number of variables including gestational age, nutrient intake, prevalence of disease, and familial characteristics

RpkA, a Highly Conserved GPCR with a Lipid Kinase Domain, Has a Role in Phagocytosis and Anti-Bacterial Defense

RpkA (Receptor phosphatidylinositol kinase A) is an unusual seven-helix transmembrane protein of Dictyostelium discoideum with a G protein coupled receptor (GPCR) signature and a C-terminal lipid kinase domain (GPCR-PIPK) predicted as a phosphatidylinositol-4-phosphate 5-kinase. RpkA-homologs are present in all so far sequenced Dictyostelidae as well as in several other lower eukaryotes like the oomycete Phytophthora, and in the Legionella host Acanthamoeba castellani. Here we show by immunofluorescence that RpkA localizes to endosomal membranes and is specifically recruited to phagosomes. RpkA interacts with the phagosomal protein complex V-ATPase as proteins of this complex co-precipitate with RpkA-GFP as well as with the GST-tagged PIPK domain of RpkA. Loss of RpkA leads to a defect in phagocytosis as measured by yeast particle uptake. The uptake of the pathogenic bacterium Legionella pneumophila was however unaltered whereas its intra-cellular replication was significantly enhanced in rpkA-. The difference between wild type and rpkA- was even more prominent when L. hackeliae was used. When we investigated the reason for the enhanced susceptibility for L. pneumophila of rpkA- we could not detect a difference in endosomal pH but rpkA- showed depletion of phosphoinositides (PIP and PIP2) when we compared metabolically labeled phosphoinositides from wild type and rpkA-. Furthermore rpkA- exhibited reduced nitrogen starvation tolerance, an indicator for a reduced autophagy rate. Our results indicate that RpkA is a component of the defense system of D. discoideum as well as other lower eukaryotes

Structural characterization suggests models for monomeric and dimeric forms of full-length ezrin

Ezrin is a member of the ERM (ezrin–radixin–moesin) family of proteins that have been conserved through metazoan evolution. These proteins have dormant and active forms, where the latter links the actin cytoskeleton to membranes. ERM proteins have three domains: an N-terminal FERM [band Four-point-one (4.1) ERM] domain comprising three subdomains (F1, F2, and F3); a helical domain; and a C-terminal actin-binding domain. In the dormant form, FERM and C-terminal domains form a stable complex. We have determined crystal structures of the active FERM domain and the dormant FERM:C-terminal domain complex of human ezrin. We observe a bistable array of phenylalanine residues in the core of subdomain F3 that is mobile in the active form and locked in the dormant form. As subdomain F3 is pivotal in binding membrane proteins and phospholipids, these transitions may facilitate activation and signaling. Full-length ezrin forms stable monomers and dimers. We used small-angle X-ray scattering to determine the solution structures of these species. As expected, the monomer shows a globular domain with a protruding helical coiled coil. The dimer shows an elongated dumbbell structure that is twice as long as the monomer. By aligning ERM sequences spanning metazoan evolution, we show that the central helical region is conserved, preserving the heptad repeat. Using this, we have built a dimer model where each monomer forms half of an elongated antiparallel coiled coil with domain-swapped FERM:C-terminal domain complexes at each end. The model suggests that ERM dimers may bind to actin in a parallel fashion