ayala

Yuna Ayala, PhD

Assistant Professor of Biochemistry & Molecular Biology, St. Louis University

Role of RNA processing and TDP-43 function in neurodegeneration Read More

Email: yayala@slu.edu
Lab Phone: (314) 977-9247
Keywords: neurodegeneration, amyotrophic lateral sclerosis (ALS), frontotemporal lobar degeneration (FTLD), protein aggregation, TAR DNA binding protein (TDP-43, TARDBP), RNA processing, RNA binding proteins, hnRNP

Characterizing the Role of TDP-43 in Neurodegeneration

TDP-43 function is presumably compromised upon formation of the inclusion bodies because accumulation of these cytoplasmic aggregates in patients is accompanied by nuclear clearance of the protein. The disease-associated mutations in the TARDBP gene accumulate in the C-tail downstream of the two RNA recognition domains.

My group seeks to understand how defects in RNA processing lead to human disease. In particular, we are interested in the elucidation of TDP-43 function and its connection to the development and progression of neurodegenerative disorders. TDP-43 is an RNA and DNA binding protein involved in the regulation of various RNA-associated mechanisms. TDP-43 is the main component of inclusion bodies in different types of neurodegeneration, but primarily in amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). Various lines of evidence, such as the identification of more than 40 TDP-43 mutations in ALS and FTLD patients, strongly suggest that TDP-43 dysfunction contributes to neurodegeneration. Despite the significant recent progress in the elucidation of TDP-43 function, the related processes that play a role in pathogenesis remain unknown. Our goals are to determine cellular pathways that regulate TDP-43, to define models of TDP-43-mediated RNA processing, and to understand their connection to disease.

Updated January 2014

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