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Investigador
Yolanda Sanchez
Universidad
UNIVERSIDAD DE SALAMANCA FACULTAD DE BIOLOGIA
Trabajos
37 trabajos publicados.
Último trabajo publicado(2021-10): Detection of surface forces by the cell-wall mechanosensor Wsc1 in yeast
Último trabajo publicado(2021-10): Detection of surface forces by the cell-wall mechanosensor Wsc1 in yeast
Tecnologías
Descripcion
My experience is based on what today we could call "functional biology" in yeasts. I began studying secretion in Luis Rodriguez laboratory at the University of Salamanca, where we intend to understand the genetic system controlling the synthesis of invertase. During the Postdoc, I worked in the field of "heat-shock proteins” in Susan Lindquist laboratory at the University of Chicago. This was the moment when the term “chaperone” was coined and my work contributed to the characterization of Hsp104 (heat-shock protein 104), the first “heat-shock” protein required for thermotolerance in yeasts (Sanchez and Lindquist, Science 1990; Parsell et al., Nature, 1991, Sanchez et al., EMBO J, 1992). Previously, it had been seen that these proteins were induced with increasing temperature, but until that moment, neither of them (Hsp70 nor Hsp83), had been shown to participate in tolerance to high temperatures. Interestingly a few years later, Hsp104 was shown to be necessary for the propagation of PSI+ and other prions in S. cerevisiae. This period was very useful to begin to understand the mechanisms that control the stress response in yeasts.Later, I joined the “cell wall” group coordinated by Dr. Angel Durán in Salamanca and began to study the biosynthesis of the cell wall in S. pombe. To tackle this problem, with my first PhD student we decided to look for new regulators of the process. We performed a “screening” of S. pombe mutants hypersensitive to the antifungals echinocandin and calcofluor. This is how we obtained the mutants ehs1-1 and ehs2-1 (echinocandin hypersensitive) (Carnero et al, MGG, 2001), one of which has been basic for the research we carry out later on in the laboratory. We have identified and characterized the catalytic subunits of -glucan synthase (GS), Bgs2, Bgs3 and Bgs4 (Martin et al, Mol. Microbiol, 2000, Martin el al, Eukaryotic Cell. 2003, Cortés et al, J.Cell Sci . 2005) and some -glucan synthases (GS), Mok11, Mok12, Mok13 and Mok14 (Garcia et al., Mol Microbiol, 2005).From one of the hypersensitive mutants (ehs2-1), we identified rgf3+ and the contiguous ORF in the rgf1+ genome, both encoding Rho-GEFs of the GTPase Rho1p (Tajadura, et al., J. Cell. Sci. 2004; Garcia et al., Yeast, 2006b). Rho1p is involved in many essential processes. However, with the exception of its role as an activator of β-GS, its specific contribution to processes such as polarity or cell integrity was unknown 15 years ago. We found that Rgf2p is a Rho1-GEF specific of sporulation (Garcia et al., Genetics, 2009b). In addition, the characterization of the rgf1+ mutants, has allowed us to propose new functions of Rho1p, such as its involvement in the transition from monopolar to bipolar growth (Garcia et al., MBoC 2006a) and its role in the regulation of the cell integrity pathway (Garcia et al., MBoC, 2009a). Along the same line, we have seen that Rgf1p accumulates in the nucleus in response to replicative stress and that this accumulation depends on the checkpoint of S phase (Muñoz, et al., MBoC, 2014). This work has opened new lines of research that explore the role of Rho1p and its activators in the DNA Damage Response. We have shown the participation of Rgf1p in the repair process of DSBs caused by Fleomycin (Manjon et al, NAR, 2017). More recently, when exploring the role of Rgf1 in cytokinesis, we found that Rgf1p and the CIP pathway, together with the septation initiation network (SIN), participate in a checkpoint that guarantees cytokinesis under cell wall stress conditions (Edreira et al, eLife, 2020).