“In insects, the antenna consists of a scapus, a pedicellus, and a flagellum comprising selleck kinase inhibitor many segments (flagellomeres).
These segments possess many morphological types of sensory organs (sensilla) to process multimodal sensory information. We observed the sensilla on flagellomeres in praying mantis (Tenodera aridifolia) with both scanning and transmission electron microscopes. We classified the sensilla into six types: chaetic,.campaniform, coelocapitular, basiconic, trichoid and grooved peg sensilla, and inferred their presumptive functions on the basis of their external and internal structures. In addition, based on their distribution, we newly divided the flagellum into 6 distinct parts. This new division leads to a better understanding about the sexual dimorphism and the antennal development in the mantises. The sexual difference in distribution of the grooved peg sensilla suggests that this type of sensilla may play a role in sex-pheromone detection in mantis, which is a rare case of double-walled sensilla mediating this function. (C) 2013 Elsevier Ltd. All rights reserved.”
“Protein kinase B
(PKB; also known as Akt) is important for mediating survival and proliferation signals. Following activation, PKB shuttles to Various compartments of the cell, including the nucleus, where it phosphorylates an array of targets. PKB is phosphorylated at T308 by its activator PDK1. PDK1 P5091 in vivo is normally excluded from the nucleus via a nuclear exclusion sequence (NES), and our previous work suggested that nuclear exclusion can be attenuated by IGF-1-induced phosphorylation of S396 proximal to MX69 mouse the NES. No studies have been done to test the significance of S396 phosphorylation or the impact of nuclear accumulation of PDK1 on PKB activation. To address these questions,
we created isogenic embryonic stem cell (ESC) lines expressing various alleles of PDK1 within a PDK1-/- background. Disruption of the NES domain of PDK1 Correlated with elevated PKB phosphorylation at both T308 and S473. In contrast, mutation of S396 to alanine reduced PDK1 nuclear localization and reduced PKB phosphorylation and activation. The loss of phosphorylation of PKB by S396A mutation was rescued by forcing nuclear PDK1 or by conversion of S396 to an aspartic acid. The phosphorylation of the PKB substrate FOXO3 alpha was reduced in S396A PDK1 ESC. Other known and suspected PKB substrates, including GSK3 and Raf1, were unaffected. This Study therefore reveals that S396 plays a role in the activation of PKB leading to the regulated phosphorylation of some PKB substrates including FOXO3 alpha. (c) 2008 Elsevier Inc. All rights reserved.”
“Cells continually assess their energy and nutrient state to maintain growth and survival and engage necessary homeostatic mechanisms. Cell-autonomous responses to the fed state require the surveillance of the availability of amino acids and other nutrients.