Professional Education

  • Bachelor of Science, Pennsylvania State University (2012)
  • Doctor of Philosophy, Cornell University (2019)
  • PhD, Cornell University, Biochemistry, Molecular, and Cell Biology (2019)

Stanford Advisors

All Publications

  • Whi5 is diluted and protein synthesis does not dramatically increase in pre-Start G1. Molecular biology of the cell Schmoller, K. M., Lanz, M. C., Kim, J., Koivomagi, M., Qu, Y., Tang, C., Kukhtevich, I. V., Schneider, R., Rudolf, F., Moreno, D. F., Aldea, M., Lucena, R., Skotheim, J. M. 2022; 33 (5): lt1

    View details for DOI 10.1091/mbc.E21-01-0029

    View details for PubMedID 35482510

  • In-depth and 3-dimensional exploration of the budding yeast phosphoproteome EMBO REPORTS Lanz, M. C., Yugandhar, K., Gupta, S., Sanford, E. J., Faca, V. M., Vega, S., Joiner, A. N., Fromme, J., Yu, H., Smolka, M. B. 2021: e51121


    Phosphorylation is one of the most dynamic and widespread post-translational modifications regulating virtually every aspect of eukaryotic cell biology. Here, we assemble a dataset from 75 independent phosphoproteomic experiments performed in our laboratory using Saccharomyces cerevisiae. We report 30,902 phosphosites identified from cells cultured in a range of DNA damage conditions and/or arrested in distinct cell cycle stages. To generate a comprehensive resource for the budding yeast community, we aggregate our dataset with the Saccharomyces Genome Database and another recently published study, resulting in over 46,000 budding yeast phosphosites. With the goal of enhancing the identification of functional phosphorylation events, we perform computational positioning of phosphorylation sites on available 3D protein structures and systematically identify events predicted to regulate protein complex architecture. Results reveal hundreds of phosphorylation sites mapping to or near protein interaction interfaces, many of which result in steric or electrostatic "clashes" predicted to disrupt the interaction. With the advancement of Cryo-EM and the increasing number of available structures, our approach should help drive the functional and spatial exploration of the phosphoproteome.

    View details for DOI 10.15252/embr.202051121

    View details for Web of Science ID 000610988800001

    View details for PubMedID 33491328

    View details for PubMedCentralID PMC7857435