Susan Marqusee

About

Susan Marqusee is a Professor at the University of California Berkeley, affiliated with the Department of Molecular and Cell Biology and the California Institute for Quantitative & Biological Sciences. She serves as the Principal Investigator of the Marqusee Lab, where her research focuses on understanding the molecular mechanisms underlying protein folding, stability, and function. Her work aims to elucidate how proteins maintain their structure and activity under various cellular conditions, which has implications for understanding diseases related to protein misfolding and developing therapeutic strategies.

Research topics

• Biology
• Biophysics
• Biochemistry
• Genetics
• Chemistry
• Cell biology
• Virology
• Medicine
• Crystallography
• Computational biology

Selected publications

• Multivalent interactions between CsoS2 and Rubisco mediate α-carboxysome formation

  Nature Structural & Molecular Biology · 2020 · 165 citations

  DOI

• The SARS-CoV-2 spike reversibly samples an open-trimer conformation exposing novel epitopes

  Nature Structural & Molecular Biology · 2022 · 163 citations

  Senior authorCorresponding
  PublisherOA PDFDOI

• Identification of a conserved S2 epitope present on spike proteins from all highly pathogenic coronaviruses

  eLife · 2023 · 85 citations

  To address the ongoing SARS-CoV-2 pandemic and prepare for future coronavirus outbreaks, understanding the protective potential of epitopes conserved across SARS-CoV-2 variants and coronavirus lineages is essential. We describe a highly conserved, conformational S2 domain epitope present only in the prefusion core of β-coronaviruses: SARS-CoV-2 S2 apex residues 980-1006 in the flexible hinge. Antibody RAY53 binds the native hinge in MERS-CoV and SARS-CoV-2 spikes on the surface of mammalian cell…

  PublisherDOI

• Stepwise activation of a metabotropic glutamate receptor

  Nature · 2024-04-17 · 35 citations

  articleOpen access
  PublisherOA PDFDOI

• NUB1 traps unfolded FAT10 for ubiquitin-independent degradation by the 26S proteasome

  Nature Structural & Molecular Biology · 2025-04-11 · 11 citations

  articleOpen access

  The ubiquitin-like modifier FAT10 targets hundreds of proteins in the mammalian immune system to the 26S proteasome for degradation. This degradation pathway requires the cofactor NUB1, yet the underlying mechanisms remain unknown. Here, we reconstituted a minimal in vitro system with human components and revealed that NUB1 uses the intrinsic instability of FAT10 to trap its N-terminal ubiquitin-like domain in an unfolded state and deliver it to the 26S proteasome for engagement, allowing the de…

  PublisherOA PDFDOI

Recent grants

• Single Molecule Studies of Protein Folding

  NSF · $1.2M · 2011–2017

• Project 2: Conformation and propagation of misfolded forms of tau and Abeta

  NIH · $84.7M · 1997–2026

• NIH Grant R29GM050945

  NIH · $517k · 1999

Frequent coauthors

• Carlos Bustamante

  University of California, Berkeley

  78 shared

• John Kuriyan

  Vanderbilt University

  58 shared

• Neel H. Shah

  Columbia University

  45 shared

• Christine L. Gee

  Howard Hughes Medical Institute

  45 shared

• Kambiz M. Hamadani

  California State University, San Marcos

  44 shared

• Shion A. Lim

  42 shared

• Jamie H. D. Cate

  University of California, Berkeley

  37 shared

• Emily J. Guinn

  Eli Lilly (United States)

  35 shared

Labs

• The Marqusee LabPI

  Not provided

Education

• PhD, Biochemistry

  Stanford University School of Medicine

  1990

• MD

  Stanford University School of Medicine

  1990

• AB, Physics and Chemistry

  Cornell University

  1982

Similar researchers at University of California, Berkeley

• Peidong Yangh-262
• Jennifer A. Doudnah-230
• Jeffrey R. Longh-189