The Molecular Basis and Biologic Significance of the β-Dystroglycan-Emerin Interaction.

β-dystroglycan (β-DG) assembles with lamins A/C and B1 and emerin at the nuclear envelope (NE) to maintain proper nuclear architecture and function. To provide insight into the nuclear function of β-DG, we characterized the interaction between β-DG and emerin at the molecular level. Emerin is a major NE protein that regulates multiple nuclear processes and whose deficiency results in Emery-Dreifuss muscular dystrophy (EDMD).

The intracellular domain of β-dystroglycan mediates the nucleolar stress response by suppressing UBF transcriptional activity.

β-dystroglycan (β-DG) is a key component of multiprotein complexes in the plasma membrane and nuclear envelope. In addition, β-DG undergoes two successive proteolytic cleavages that result in the liberation of its intracellular domain (ICD) into the cytosol and nucleus. However, stimuli-inducing ICD cleavage and the physiological relevance of this proteolytic fragment are largely unknown.

Determination of toxicity levels in the San Pedro River Watershed, Aguascalientes, Mexico.

A quantitative study of toxicity levels of the San Pedro River and its main tributaries around the city of Aguascalientes, Mexico was conducted. Our study determined individual CL(50) values for each sampling point at 3 different times of the year corresponding to the main seasons of the year in terms of the hydrological cycle (dry, low rain and high rain season). Those LC(50) values were used to calculate the acute.