Patrick Lombardi
Mount St. Mary's University, MD·Biochemistry
Cells constantly need to send repair crews to the right place at the right time. One way they do this is by tagging damaged sites with chains of ubiquitin, a small protein that acts like a molecular label.
- Fields
Biochemistry
Biophysics
Chemistry
- Topics
ubiquitin
CUE domain
ALKBH3-ASCC
- Grants
- 1 known grant, last ended Aug 2026
What they work on
- Identify the specific molecular contacts between the ASCC2 CUE domain, a small ubiquitin-binding module, and K63-linked polyubiquitin chains, using NMR spectroscopy to report on atom-level interactions.
- Build an integrative structural model of ASCC2 bound to K63-linked chains that agrees with NMR, mutagenesis and small angle X-ray scattering (SAXS) data, which shows overall molecular shape.
- Measure whether the predicted ASCC2–polyubiquitin contacts matter for function, using in vitro binding assays and cell-based assays.
- Explain why ASCC2 prefers K63-linked chains over the many other ubiquitin chain types in the cell, and how this targets repair complexes such as ALKBH3-ASCC.
More about the research
Different chain shapes carry different messages. Proteins that read these labels must pick out the right chain type among many. How they do this is a basic question in cell signaling. It also matters for diseases caused by faulty DNA repair.
Why it matters
Mutations that block the formation of the K63-linked chains that recruit ASCC2, or that break ASCC2's contacts within the ALKBH3-ASCC DNA repair complex, have been linked to genetic diseases. Knowing exactly how ASCC2 recognizes these chains could improve understanding of DNA damage repair and related pathways. It could also help in diagnosing diseases that arise when these pathways fail.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Gloria Borgstahl
University of Nebraska Medical Center, NE·Biochemistry
Map the proton environment of human MnSOD, an antioxidant enzyme, in its resting reduced and oxidized manganese states, using neutron crystallography at Oak Ridge National Laboratory to locate hydrogen atoms.
Penghua Wang
University of Connecticut, CT·Microbiology & Immunology
Test whether unanchored lysine 48- and lysine 63-linked ubiquitin chains bind caspase-4/11 and promote its assembly and activation, using cell-free and biochemical assays.
Morgan Stefik
University of South Carolina-Columbia, SC·Materials Science
Determine how the chemical reactivity of polymers and nanoparticles controls lasting polymer-nanoparticle binding, so that designed polymer structure-directing agents keep particles in the order they were added.
The school
Mount St. Mary's University: 1 labs on PI Pages.
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