Synaptolaemus latofasciatus, a new combination for Leporinus latofasciatus Steindachner, 1910 and its junior synonym Synaptolaemus cingulatus Myers and Fernandez-Yepez, 1950 (Characiformes: Anostomidae)

Leporinus latofasciatus was described by Steindachner (1910) on the basis of a single specimen collected in the rio Orinoco, Venezuela. Since then, no other specimen of the species was mentioned in the literature, and the species was only listed in catalogues, eventually mentioned and treated as a ""poorly known"" species, or even omitted in checklists of fishes from Venezuela. During a visit to the fish collection at the Naturhistorisches Museum at Vienna (NMW) to examine all the type specimens of Leporinus, we were able to study the holotype of Leporinus latofasciatus and recognize that the specimen corresponds to the species described by Myers and Fernandez-Yepez (in Myers, 1950) as Synaptolaemus cingulatus. Thus, the latter is a junior synonym of Leporinus latofasciatus and, based on that, Synaptolaemus latofasciatus (Steindachner, 1910) should be the name applied for this taxon, as a new combination. Herein new data on the holotype of Synaptolaemus latofasciatus are presented and compared with previously data from other authors. In addition, illustrations of live specimens are presented as well as new distribution records for the species.

DEPTOR Cell-Autonomously Promotes Adipogenesis, and Its Expression Is Associated with Obesity

DEP domain-containing mTOR-interacting protein (DEPTOR) inhibits the mechanistic target of rapamycin (mTOR), but its in vivo functions are unknown. Previous work indicates that Deptor is part of the Fob3a quantitative trait locus (QTL) linked to obesity/leanness in mice, with Deptor expression being elevated in white adipose tissue (WAT) of obese animals. This relation is unexpected, considering the positive role of mTOR in adipogenesis. Here, we dissected the Fob3a QTL and show that Deptor is the highest-priority candidate promoting WAT expansion in this model. Consistently, transgenic mice overexpressing DEPTOR accumulate more WAT. Furthermore, in humans, DEPTOR expression in WAT correlates with the degree of obesity. We show that DEPTOR is induced by glucocorticoids during adipogenesis and that its overexpression promotes, while its suppression blocks, adipogenesis. DEPTOR activates the proadipogenic Akt/PKB-PPAR-gamma axis by dampening mTORC1-mediated feedback inhibition of insulin signaling. These results establish DEPTOR as a new regulator of adipogenesis.

Crystal structures of Leptospira interrogans FAD-containing ferredoxin-NADP+ reductase and its complex with NADP+

Abstract Background Ferredoxin-NADP(H) reductases (FNRs) are flavoenzymes that catalyze the electron transfer between NADP(H) and the proteins ferredoxin or flavodoxin. A number of structural features distinguish plant and bacterial FNRs, one of which is the mode of the cofactor FAD binding. Leptospira interrogans is a spirochaete parasitic bacterium capable of infecting humans and mammals in general. Leptospira interrogans FNR (LepFNR) displays low sequence identity with plant (34% with Zea mays) and bacterial (31% with Escherichia coli) FNRs. However, LepFNR contains all consensus sequences that define the plastidic class FNRs. Results The crystal structures of the FAD-containing LepFNR and the complex of the enzyme with NADP+, were solved and compared to known FNRs. The comparison reveals significant structural similarities of the enzyme with the plastidic type FNRs and differences with the bacterial enzymes. Our small angle X-ray scattering experiments show that LepFNR is a monomeric enzyme. Moreover, our biochemical data demonstrate that the LepFNR has an enzymatic activity similar to those reported for the plastidic enzymes and that is significantly different from bacterial flavoenzymes, which display lower turnover rates. Conclusion LepFNR is the first plastidic type FNR found in bacteria and, despite of its low sequence similarity with plastidic FNRs still displays high catalytic turnover rates. The typical structural and biochemical characteristics of plant FNRs unveiled for LepFNR support a notion of a putative lateral gene transfer which presumably offers Leptospira interrogans evolutionary advantages. The wealth of structural information about LepFNR provides a molecular basis for advanced drugs developments against leptospirosis.