At the Weihl Lab, our goal is to understand the molecular mechanisms of protein inclusion formation, disaggregation, and clearance in myodegenerative (skeletal muscle) and neurodegenerative diseases.
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We believe that dysfunction in protein quality control (molecular chaperones) and protein degradation pathways (e.g. the ubiquitin proteasome system, autophagy and endocytosis) disrupt cellular protein homeostasis resulting in degenerative phenotypes and normal aging. We employ complementary experimental techniques such as biochemistry, cell culture, animal models, and patient tissue to achieve these goals.
Our lab is particularly interested in the pathogenesis of inclusion body myopathy, paget’s disease of the bone and frontotemporal dementia or IBMPFD, a multisystem degenerative disorder due to missense mutations in p97/VCP/cdc48. IBMPFD muscle and brain tissue contains ubiquitinated protein inclusions associated with cellular degeneration and vacuolation.
Zhang X, Sergin I, Evans TD, Jeong SJ, Rodriguez-Velez A, Kapoor D, Chen S, Song E, Holloway KB, Crowley JR, Epelman S, Weihl CC, Diwan A, Fan D, Mittendorfer B, Stitziel NO, Schilling JD, Lodhi IJ, Razani B.
Nat Metab. 2020 Sep;2(9):991. doi: 10.1038/s42255-020-00291-6
Lin AY, Siener CS, Faino AV, Seiffert M, Weihl CC, Wang LH.
Neuromuscul Disord. 2020 Aug 19:S0960-8966(20)30555-1. doi: 10.1016/j.nmd.2020.08.358. Online ahead of print.
Bengoechea R, Findlay AR, Bhadra AK, Shao H, Stein KC, Pittman SK, Daw J, Gestwicki JE, True HL, Weihl CC.
J Clin Invest. 2020 May 19:136167. doi: 10.1172/JCI136167. Online ahead of print.
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