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

Azuara-Medina, Paulina Margarita ; Sandoval-Duarte, Ariana María ; Morales-Lázaro, Sara L. ; Modragón-González, Ricardo ; Vélez-Aguilera, Griselda ; Gómez-López, Juan de Dios ; Jiménez-Gutiérrez, Guadalupe Elizabeth ; Tiburcio-Félix, Reynaldo ; Martínez-Vieyra, Ivette ; Suárez-Sánchez, Rocío ; Längst, Gernot ; Magaña, Jonathan Javier ; Winder, Steve J. ; Ortega, Arturo ; Ramos Perlingeiro, Rita de Cassia ; Jacobs, Laura A. ; Cisneros, Bulmaro



Abstract

beta-dystroglycan (beta-DG) is a key component of multiprotein complexes in the plasma membrane and nuclear envelope. In addition, beta-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 ...

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