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Jennifer Rauch

Assistant Professor of Biochemistry & Molecular Biology

Research areas focus on the mechanisms of protein misfolding, aggregation, and spread in neurodegenerative disease.

Current Research
The Rauch lab is focused on understanding the cellular and molecular mechanisms that contribute to diseases associated with protein misfolding and aggregation - with a particular focus on the neurodegenerative protein tau. Tau is an abundant and highly soluble protein, yet is known to aggregate in a variety of diseases, including Alzheimer’s Disease. The deposition of tau aggregates, or neurofibrillary tangles (NFTs), is correlated with cognitive decline in patients and permits neuropathological diagnoses of patients in different stages of disease. While the composition and structure of NFTs are well-characterized, the in vivo process of tau aggregation and the subsequent spread of this aggregation are not well understood phenomena.

The lab is focused on three main areas of research in regards to tau neurobiology: tau spread mechanisms, tau physical state transitions, and the influence of cellular identity on disease mechanism. The overarching goal of the lab is to understand the requirements for tau disease progression and to devise new strategies to treat disease. We use a variety of techniques in the lab (in vitro biochemistry, single cell RNA sequencing, CRISPR-based functional genomics, optogenetic technologies, etc.) across different system models (cell lines, differentiated stem cells, primary cultures, and mice) in order to build a complete picture of tau regulation.

Learn more at https://www.biochem.umass.edu/faculty/jennifer-rauch

Academic Background

  • PhD: University of Michigan
  • Postdoctoral Training: University of California, Santa Barbara
Rauch JN, Luna G, Guzman E, Audouard M, Challis C, Sibih YE, Leshuk C, Hernandez I, Wegmann S, Hyman BT, Gradinaru V, Kampmann M, Kosik KS. LRP1 is a master regulator of tau uptake and spread. Nature. 2020; 580: 381–385.
Zhang X, Vigers M, McCarty J, Rauch JN, Fredrickson GH, Wilzon MZ, Shea JE, Han S, Kosik KS. The proline-rich domain promotes Tau liquid liquid phase separation in cells. J Cell Biol. 2020; 219(11): e202006054.
Lin Y*, McCarty J*, Rauch JN, Kosik KS, Fredrickson GH, Shea JE, Han S. Narrow equilibrium window for the complex coacervation of tau and RNA under cellular conditions. eLife. 2019; pii: e42571.
Hernandez I*, Luna G*, Rauch JN, Reis SA, Giroux M, Karch CM, Boctor D, Sibih YE, Storm NJ, Diaz A, Kaushik S, Zekanowski C, Kang AA, Hinman CR, Cerovac V, Guzman E, Zhou H, Haggarty SJ, Goate AM, Fisher SK, Cuervo AM, Kosik KS. A farnesyltransferase inhibitor activates lysosomes and reduces tau pathology in mice with tauopathy. Science Translational Medicine. 2019; 11(485). pii: eaat3005.
Fichou Y*, Lin Y*, Rauch JN, Vigers M, Kosik KS, Han S. Cofactors are essential consituents of stable and seeding-active tau fibrils. PNAS. 2018; 115(52): 13234-13239.
Rauch JN, Chen JJ, Sorum A, Miller GM, Sharf T, See SK, Hsieh-Wilson LC, Kampmann M, Kosik KS. Tau internalization is regulated by 6-O sulfation on Heparan Sulfate Proteoglycans (HSPGs). Scientific Reports. 2018; 8(1): 6382.
Mok SA, Condello C, Freilich R, Gillies A, Arhar T, Oroz J, Kadavath H, Julien O, Assimon VA, Rauch JN, Dunyak BM, Lee J, Tsai FTF, Wilson MR, Zweckstetter M, Dickey CA, Gestwicki JE. Mapping Interactions with the Chaperone Network Reveals Factors that Protect Against Tau Aggregation. Nature Structural & Molecular Biology. 2018; 25(5):384-393.
Zhang X, Lin Y, Eschmann NA, Zhou H, Rauch JN, Hernandez I, Guzman E, Kosik KS, Han S. RNA stores tau reversibly in complex coacervates. PLoS Biology. 2017; 15(7): e2002183.
Rauch JN, Olson SH, Gestwicki JE. Interactions Between Microtubule-Binding Protein Tau (MAPT) and small molecules. Cold Spring Harb Perspect Med. 2017; 7(7): a024034.
 
Contact Info

Institute for Applied Life Sciences
N373 Life Sciences Laboratories
240 Thatcher Road
Amherst, MA 01003