Wade Harper, Ph.D.

Wade Harper, Ph.D.

Bert and Natalie Vallee Professor of Molecular Pathology (HMS)
Professor of Cell Biology (HMS)
Chair of the Department of Cell Biology (HMS)

Wade Harper, Ph.D., is the B and N Vallee Professor of Molecular Pathology, a Professor of Cell Biology, and the Chair of Cell Biology in the Blavatnik Institute at Harvard Medical School. He received his Ph.D. in Chemistry from Georgia Institute of Technology, prior to performing post-doctoral work in protein biochemistry of growth factors at Harvard Medical School. He joined the faculty in the Department of Biochemistry and Molecular Biology at Baylor College of Medicine in 1988 and subsequently moved to the Department of Pathology at Harvard Medical School (in 2003) and to the Department of Cell Biology in 2011.

The Harper Lab studies mechanisms underlying cellular homeostasis and signaling, with a focus on the ubiquitin system and the autophagy-lysosome system. The interest in the ubiquitin-proteasome system in the Harper Lab initially emerged through studies to understand how cell cycle regulators (cyclins and CDK inhibitors) are degraded to control cell cycle transitions, resulting in the discovery of cullin-RING ubiquitin ligases, and their roles in phosphorylation-dependent protein degradation. The Harper Lab currently uses quantitative proteomics, imaging, and biochemical approaches to elucidate underlying biochemical mechanisms controlling protein turnover, and applies these approaches to examine regulatory pathways relevant to various neurodegenerative disease, including Parkinson’s and Alzheimer’s diseases. A major focus currently is the PARKIN ubiquitin ligase, which controls turnover of damaged mitochondria via the autophagy pathway and is mutated in Parkinson’s Disease. The Harper Lab, together with the Gygi Lab at HMS, is also using proteomics to develop a large-scale human protein interaction network including the majority of proteins encoded by the human genome.

Harvard Medical School

Dept. of Cell Biology, C-462A

240 Longwood Avenue

Boston, MA 02115

Lab telephone: 617-432-6590

The X-linked intellectual disability protein PHF6 associates with the PAF1 complex and regulates neuronal migration in the mammalian brain.
Authors: Authors: Zhang C, Mejia LA, Huang J, Valnegri P, Bennett EJ, Anckar J, Jahani-Asl A, Gallardo G, Ikeuchi Y, Yamada T, Rudnicki M, Harper JW, Bonni A.
Neuron
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Altered social behavior and neuronal development in mice lacking the Uba6-Use1 ubiquitin transfer system.
Authors: Authors: Lee PC, Dodart JC, Aron L, Finley LW, <a href="https://connects.catalyst.harvard.edu/Profiles/profile/1242114">Bronson RT</a>, <a href="https://connects.catalyst.harvard.edu/Profiles/profile/1244863">Haigis MC</a>, <a href="https://connects.catalyst.harvard.edu/Profiles/profile/1249530">Yankner BA</a>, Harper JW.
Mol Cell
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Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Authors: Authors: Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, <a href="https://connects.catalyst.harvard.edu/Profiles/profile/1243594">Huttlin EL</a>, <a href="https://connects.catalyst.harvard.edu/Profiles/profile/1242109">Gygi SP</a>, Harper JW.
Nature
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A high-confidence interaction map identifies SIRT1 as a mediator of acetylation of USP22 and the SAGA coactivator complex.
Authors: Authors: Armour SM, Bennett EJ, Braun CR, Zhang XY, McMahon SB, <a href="https://connects.catalyst.harvard.edu/Profiles/profile/1242109">Gygi SP</a>, Harper JW, <a href="https://connects.catalyst.harvard.edu/Profiles/profile/1248897">Sinclair DA</a>.
Mol Cell Biol
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Structural conservation of distinctive N-terminal acetylation-dependent interactions across a family of mammalian NEDD8 ligation enzymes.
Authors: Authors: Monda JK, Scott DC, Miller DJ, Lydeard J, King D, Harper JW, Bennett EJ, Schulman BA.
Structure
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Comprehensive analysis of host cellular interactions with human papillomavirus E6 proteins identifies new E6 binding partners and reflects viral diversity.
Authors: Authors: White EA, Kramer RE, Tan MJ, Hayes SD, Harper JW, <a href="https://connects.catalyst.harvard.edu/Profiles/profile/1237682">Howley PM</a>.
J Virol
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Understanding cullin-RING E3 biology through proteomics-based substrate identification.
Authors: Authors: Harper JW, Tan MK.
Mol Cell Proteomics
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Cancer. Emerging anatomy of the BAP1 tumor suppressor system.
Authors: Authors: White AE, Harper JW.
Science
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Identification and proteomic analysis of distinct UBE3A/E6AP protein complexes.
Authors: Authors: Martínez-Noël G, Galligan JT, Sowa ME, Arndt V, Overton TM, Harper JW, <a href="https://connects.catalyst.harvard.edu/Profiles/profile/1237682">Howley PM</a>.
Mol Cell Biol
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SLX-1 is required for maintaining genomic integrity and promoting meiotic noncrossovers in the Caenorhabditis elegans germline.
Authors: Authors: Saito TT, Mohideen F, Meyer K, Harper JW, Colaiácovo MP.
PLoS Genet
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