The EMBO Journal (2011) 30, 3274 - 3284


Carme Solé1,3, Mariona Nadal-Ribelles1,3, Claudine Kraft2, Matthias Peter2, Francesc Posas1 and Eulàlia de Nadal1 1. Departament de Ciències Experimentals i de la Salut, Cell Signalling Unit, Universitat Pompeu Fabra (UPF), Barcelona, Spain 2. Department of Biology, Swiss Federal Institute of Technology Zurich (ETH), Institute of Biochemistry, Zurich, Switzerland 3. These authors contributed equally to this work


Protein ubiquitylation is a key process in the regulation of many cellular processes. The balance between the activity of ubiquitin ligases and that of proteases controls the level of ubiquitylation. In response to extracellular stimuli, stress-activated protein kinases (SAPK) modulate gene expression to maximize cell survival. In yeast, the Hog1 SAPK has a key role in reprogramming the gene expression pattern required for cell survival upon osmostress. Here, we show that the Ubp3 ubiquitin protease is a target for the Hog1 SAPK to modulate gene expression. ubp3 mutant cells are defective in expression of osmoresponsive genes. Hog1 interacts with and phosphorylates Ubp3 at serine 695, which is essential to determine the extent of transcriptional activation in response to osmostress. Furthermore, Ubp3 is recruited to osmoresponsive genes to modulate transcriptional initiation as well as elongation. Therefore, Ubp3 activity responds to external stimuli and is required for transcriptional activation upon osmostress.


En respuesta a estímulos extracelulares, quinasas de respuesta a estrés (SAPK) modulan la expresión génica para maximizar la supervivencia celular. En levadura, la SAPK Hog1 es responsable de coordinar esta reprogramación transcripcional en respuesta a estrés osmótico. En este trabajo se identifica la deubiquitinasa Ubp3 como una nueva diana de Hog1. En respuesta a estrés, Hog1 interaciona y fosforila Ubp3 en el residuo Ser695 modulando así la actividad deubiquitinasa y permitiendo una correcta respuesta transcripcional.

Mariona Nadal-Ribelles está realizando la tesis doctoral en el Grupo de Señalización Celular de la Universidad Pompeu Fabra dirigido por el Dr. Francesc Posas y Dra. Eulàlia de Nadal. La investigación del grupo se centra en el estudio de la vía de señalización en respuesta a estrés controlada por las MAPK de la familia de Hog1/p38, y los mecanismos moleculares que permiten una respuesta adaptativa al estrés como la regulación del ciclo celular y la transcripción.

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