Honors & Awards

  • Maximum Distinction, Universidad de Chile (2013)
  • Fondecyt (ANID) International Graduate Scholarship, Chilean Government (2014)
  • Pew Latin American Fellow, Postdoctoral Fellowship, The Pew Trusts (2020)

Professional Education

  • Bachelor of Science, Universidad de Chile, Molecular Biotechnology (2013)
  • Professional Title, Universidad de Chile, Molecular Biotechnology (Professional Engineer) (2014)
  • Doctor of Philosophy, The University of Manchester, Biotechnology, Bioscience Enterprise and Molecular Biology (2018)

Stanford Advisors

All Publications

  • Cotranslational Mechanisms of Protein Biogenesis and Complex Assembly in Eukaryotes Annual Reviews of Biomedical Data Science Morales-Polanco, F., Lee, J. H., Barbosa, N. M., Frydman, J. 2022; 5
  • Ageing exacerbates ribosome pausing to disrupt cotranslational proteostasis Nature Stein, K. C., Morales-Polanco, F., Leinden, J. v., Rainbolt, K. T., Frydman, J. 2022
  • Core Fermentation (CoFe) granules focus coordinated glycolytic mRNA localization and translation to fuel glucose fermentation. iScience Morales-Polanco, F. n., Bates, C. n., Lui, J. n., Casson, J. n., Solari, C. A., Pizzinga, M. n., Forte, G. n., Griffin, C. n., Garner, K. E., Burt, H. E., Dixon, H. L., Hubbard, S. n., Portela, P. n., Ashe, M. P. 2021; 24 (2): 102069


    Glycolysis is a fundamental metabolic pathway for glucose catabolism across biology, and glycolytic enzymes are among the most abundant proteins in cells. Their expression at such levels provides a particular challenge. Here we demonstrate that the glycolytic mRNAs are localized to granules in yeast and human cells. Detailed live cell and smFISH studies in yeast show that the mRNAs are actively translated in granules, and this translation appears critical for the localization. Furthermore, this arrangement is likely to facilitate the higher level organization and control of the glycolytic pathway. Indeed, the degree of fermentation required by cells is intrinsically connected to the extent of mRNA localization to granules. On this basis, we term these granules, core fermentation (CoFe) granules; they appear to represent translation factories, allowing high-level coordinated enzyme synthesis for a critical metabolic pathway.

    View details for DOI 10.1016/j.isci.2021.102069

    View details for PubMedID 33554071

    View details for PubMedCentralID PMC7859310

  • Glycolytic mRNAs localise and are translated in Core Fermentation (CoFe) granules to fuel glucose fermentation BioRxiv Morales Polanco, F., Bates, C., Lui, J., Solari, C., Ashe, M., et al 2020

    View details for DOI 10.1101/741231

  • Translation factor mRNA granules direct protein synthetic capacity to regions of polarized growth. The Journal of cell biology Pizzinga, M., Bates, C., Lui, J., Forte, G., Morales-Polanco, F., Linney, E., Knotkova, B., Wilson, B., Solari, C. A., Berchowitz, L. E., Portela, P., Ashe, M. P. 2019


    mRNA localization serves key functions in localized protein production, making it critical that the translation machinery itself is present at these locations. Here we show that translation factor mRNAs are localized to distinct granules within yeast cells. In contrast to many messenger RNP granules, such as processing bodies and stress granules, which contain translationally repressed mRNAs, these granules harbor translated mRNAs under active growth conditions. The granules require Pab1p for their integrity and are inherited by developing daughter cells in a She2p/She3p-dependent manner. These results point to a model where roughly half the mRNA for certain translation factors is specifically directed in granules or translation factories toward the tip of the developing daughter cell, where protein synthesis is most heavily required, which has particular implications for filamentous forms of growth. Such a feedforward mechanism would ensure adequate provision of the translation machinery where it is to be needed most over the coming growth cycle.

    View details for DOI 10.1083/jcb.201704019

    View details for PubMedID 30877141