Targeting Protein Misfolding and ER Stress in Neurodegenerative Disease


Several neurodegenerative disorders, including Alzheimer’s disease, Parkinson’s disease, Huntington’s disease, and ALS share common features, most notably the accumulation of misfolded protein aggregates. The buildup of damaged protein inclusions results in activation of cellular stress responses emerging from the endoplasmic reticulum (ER). Recent findings place ER stress as a key component of neurodegeneration, highlighting the importance of understanding this signaling pathway. This project will combine multi-disciplinary approaches including high content cell-based screening, quantitative imaging, cell biological assays, and in vitro protein biochemistry to characterize the pathways that modulate and lead to neurodegeneration caused by protein misfolding and ER stress.


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Manford, A., Stefan, C.J., MacGurn, J., Yuan, H., and S.D. Emr, (2012). ER-PM tethering proteins regulate cell signaling and ER morphology. Dev Cell, 23: 1129-1140.


 Nishimura A.L., et al., (2004) A mutation in the vesicle-trafficking protein VAPB causes late-onset spinal muscular atrophy and amyotrophic lateral sclerosis. Am J Hum Genet., 75: 822–831.


Walker, A., and Atkin, J., (2011) Stress signaling from the endoplasmic reticulum: A central player in the pathogenesis of amyotrophic lateral sclerosis. IUBMB Life., 9: 754-763.

Biological Areas:

Cell Biology


Animal disease, health and welfare