Lamin A Ser404 is a nuclear target of Akt phosphorylation in C2C12 cells

Akt/PKB is a central activator of multiple signaling pathways coupled with a large number of stimuli. Although both localization and activity of Akt in the nuclear compartment are well-documented, most Akt substrates identified so far are located in the cytoplasm, while nuclear substrates have remained elusive. A proteomic-based search for nuclear substrates of Akt was undertaken, exploiting 2D-electrophoresis/MS in combination with an anti-Akt phosphosubstrate antibody. This analysis indicated lamin A/C as a putative substrate of Akt in C2C12 cells. In vitro phosphorylation of endogenous lamin A/C by recombinant Akt further validated this result. Moreover, by phosphopeptide analysis and point mutation, we established that lamin A/C is phosphorylated by Akt at Ser404, in an evolutionary conserved Akt motif. To delve deeper into this, we raised an antibody against the lamin A Ser404 phosphopeptide which allowed us to determine that phosphorylation of lamin A Ser404 is triggered by the well-known Akt activator insulin, and is therefore to be regarded as a physiological response. Remarkably, expression of S404A lamin A in primary cells from healthy tissue caused the nuclear abnormalities that are a hallmark of Emery-Dreifuss muscular dystrophy (EDMD) cells. Indeed, it is known that mutations at several sites in lamin A/C cause autosomal dominant EDMD. Very importantly, we show here that Akt failed to phosphorylate lamin A/C in primary cells from an EDMD-2 patient with lamin A/C mutated in the Akt consensus motif. Together, our data demonstrate that lamin A/C is a novel signaling target of Akt, and implicate Akt phosphorylation of lamin A/C in the correct function of the nuclear lamina.     

Selectivity enhancement induced by substitution of non-natural analogues of arginine and lysine in arginine-based thrombin inhibitors.

Seven non-natural analogues of arginine and lysine have been substituted in an established arginine-based thrombin inhibitor. Four of the new compounds exhibited significant thrombin inhibition (K(i)'s 0.53-3.95 microM) and were subsequently tested for selectivity against trypsin. The two best compounds gave selectivity ratios of 962 and 525 (trypsin/thrombin), improving upon the parent compound.     

应用附加绿黄色光二极管的黄色胶片监测温室中的粉虱、蚜虫和蕈蚊

绿黄色光二极管(LED)附加在塑胶杯和胶片捕捉器可增加捕捉实验室和温室中昆虫的数量。附加有530nm绿黄色LED的塑胶杯捕捉器比没有附加的捕捉到更多的Trialeurodes vaporariorum(Westwood)和Bemisia tabaci(Gennadius)B生态型。在温室中昆虫笼以四季豆和棉花试验,附加有530nm绿黄色LED的黄色胶片(YC)和透明塑胶片(CS)分别缩写为LED—YC和LED—CS)比每一种没有附加的捕捉器捕捉到更多的T.vaporariorum,B．tabaci B生态型,Ahis gossypii(Glover)和Bradysia coprophila(Lintner)成虫。绿黄色LED—YC在温室中有用为监测和控制的潜在性。     

Studying the Logone floodplain,Cameroon, as a coupled human and natural system§

African floodplains are an excellent example of coupled human–natural systems because they exhibit strong interactions among multiple social, ecological, and hydrological systems. The intra-annual and interannual variations in seasonal flooding have direct and indirect impacts on ecosystems and human lives and livelihoods. Coupled human and natural system (CHANS) is a broad conceptual framework that is used to study systems in which human and natural components interact. While there are other conceptual frameworks to study social-ecological systems, the CHANS framework offers a clear way of studying the interactions, called couplings, between human and natural systems. Core features of the framework are the following: human and natural systems are analytically separated; focus is on processes within and couplings between systems; and the goal is to build an integrative, quantitative model of the coupled system. This paper explains the conceptual framework of coupled systems, using the case study of the Logone floodplain in Cameroon. We compare the CHANS framework with other frameworks that have been used to study the same floodplain, and argue for its usefulness in the study of African floodplains.