Simulating Future Urban Expansion in Monastir, Tunisia, as an Input for the Development of Future Risk Scenarios

Under scenarios of urbanization coupled with increasing frequency and intensity of natural hazards, urban disaster risk is set to rise. Simulating future urban expansion can provide relevant information for the development of future exposure scenarios and the identification of targeted risk reduction and adaptation strategies. Here, we present an urban growth simulation for the coastal city of Monastir, Tunisia. The approach integrates local knowledge and a data-driven urban growth model to simulate urban sprawl up to 2030. A business-as-usual projection is used to predict the future growth of the city based on the historical trend. Thirteen Landsat images for the period 1975 to 2017 were used to delineate past changes in urban land cover following the European Urban Atlas standard, which served as the main input for the urban growth model. The simulation revealed that the city’s residential area is likely to grow by 127 ha to an overall size of 1,690 ha by 2030, corresponding to an increase of 8.1% compared to the urban footprint of 2017. The outcomes of the analysis presented here served as an input for the spatial simulation of future exposure to flash floods in the case study area

ADAM10, the Rate-limiting Protease of Regulated Intramembrane Proteolysis of Notch and Other Proteins, Is Processed by ADAMS-9, ADAMS-15, and the γ-Secretase*S⃞

ADAM10 is involved in the proteolytic processing and shedding of proteins such as the amyloid precursor protein (APP), cadherins, and the Notch receptors, thereby initiating the regulated intramembrane proteolysis (RIP) of these proteins. Here, we demonstrate that the sheddase ADAM10 is also subject to RIP. We identify ADAM9 and -15 as the proteases responsible for releasing the ADAM10 ectodomain, and Presenilin/γ-Secretase as the protease responsible for the release of the ADAM10 intracellular domain (ICD). This domain then translocates to the nucleus and localizes to nuclear speckles, thought to be involved in gene regulation. Thus, ADAM10 performs a dual role in cells, as a metalloprotease when it is membrane-bound, and as a potential signaling protein once cleaved by ADAM9/15 and the γ-Secretase