Natura Myeku, Ph.D.

Assistant Professor of Pathology and Cell Biology
Columbia University

Dr. Myeku completed her master of science degree at Weill Cornell Medical College and her Ph.D. at The Graduate Center, The City University of New York. She then began her postdoctoral work at Columbia University, which she completed in 2013. Her research is aimed at understanding the role of deficient protein quality control in tauopathy disorders that have a common feature—accumulation of aberrant misfolded tau. There is therapeutic potential, as clearance of misfolded proteins at an early stage of tauopathy or in combination with other therapies may be clinically beneficial.

Dr. Myeku identified a therapeutic strategy acting through the cyclic adenosine monophosphate/protein kinase A (cAMP/PKA) pathway to enhance the function of the ubiquitin-proteasome system (UPS) in mouse models of tauopathy. This study suggests that protein clearance approaches also may have potential therapeutic application for other proteinopathy disorders. The study was published in Nature Medicine 2016, and also was featured in Nature Medicine News & Views.

During her graduate studies, Dr. Myeku was a recipient of the NIH-TL1 training award (2008–2011) from Weill Cornell Medical College, granted only to outstanding upcoming basic scientists who showed that their research had a novel clinical application.

In addition to her experience in understanding the mechanisms of age-related neurodegenerative diseases, Dr. Myeku also is interested in translational research. Utilizing her current expertise in transgenic mouse models and her background in translational research, she plans to fully devote her career to becoming a leader in translational neuroscience, where new discoveries hopefully can be translated swiftly into new therapies for neurodegenerative diseases.

Funded Research

Project Description Researchers Funding
Propagation of Tauopathy and Ubiquitin Proteasome System Dysfunction: Impact and Rescue with a UPS Activator

The brain of a patient with Alzheimer’s disease shows two abnormalities: clumps of a protein called amyloid into what is known as amyloid plaques, and clumps of a protein called tau into what is known as neurofibrillary tangles. One of the features of Alzheimer’s disease is that the tangles start in one part of the brain (areas involved in memory and learning), but they infect new regions and spread through the brain, contributing to the worsening of the disease.