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Edwin W. Taylor

Dr. Edwin W. Taylor is an American scientist and adjunct professor of cell and developmental biology at Northwestern University in the Feinberg School of Medicine. Known as the “father of cytoskeletal research,” his early work was once deemed controversial but is now some of the principle concepts of cellular biology.

Education

Taylor obtained a PhD from the University of Chicago in 1957, working under research mentor Dr. William Bloom. At the time, his work was primarily focused on measuring rates of mitotic processes using polarized light microscopy to visualize the spindles as they formed. In 1959, Dr. Taylor pursued his postdoctoral fellowship at Massacheusetts Institute of Technology (MIT) under the guidance of Francis O. Schmitt. Here, he gained experience in protein chemistry and studied the properties of intermediate filaments. Later in life, he also spent some of his career at the Medical Research Council Muscle Unit at Kings College in London.

Dr. Taylor previously worked at his alma mater, The University of Chicago, and was the Louis Block Professor of Molecular Genetics and Cell Biology and tenured professor of biochemistry and molecular biology. Here, his laboratory studied filamentous proteins and models of mitosis.  In 1999, Taylor transitioned into a part time position at The University of Chicago and shared his remaining time in the Gary Borisy laboratory at Northwestern University.

A dipiction of mitosis occuring in the cell, a concept studied by Dr. Taylor.

Research and Career

Research interests and Publications

Dr. Edwin Taylors general research interests include investigating the molecular mechanisms behind the movement of cells. During his early research at the University of Chicago, Dr. Taylor was primarily focused on studying the mitotic apparatus. Using colchicine, he and his students showed that the 6S colchicine binding protein is the subunit of microtubules. One of his students, Richard Weisenberg, went on to successfully use a clinching experiment to polymerize tubulin into microtubules. Moving forward, his next research question focused on what moves chromosomes. Here, his lab was one of the first to work on the similarities between non-muscle and muscle actin. From this point forward, Dr. Taylor has delved into the role of actin and myosin in muscle contraction, as well as cell movement.

His laboratory uses biochemical and biophysical methods to study how ATP hydrolysis can be used to generate force. Using skeletal muscle, his group discovered a model for the mechanism of actomyosin ATPase and its relationship to the contraction cycle, providing the first kinetic model showing how molecular motors convert energy into mechanical force. His work also uncovered the protein subunits of microtubules. Currently, Dr. Taylor and his group are looking into the mechanochemical properties of the cytoskeleton using the same methods prepared for their study of motor proteins.

Dr. Taylor’s most recent research interests can be seen in a publication by the Journal of General Physiology titled “Investigation into the mechanism of thin filament regulation by transient kinetics and equilibrium binding: Is there a conflict?” In this study, the relationship between thin filament regulation and binding of ligands are evaluated in the muscle contraction cycle. This research uses a fast-mixing instrument to further study the precise mechanisms of regulation and sort any theoretical conflicts. The main regulatory point in this process is the removal of inorganic phosphate, which participates in the kinetic pathway and is accelerated one-hundred-fold using the association of ligands like calcium and myosin heads with the thin filaments. However, their findings show the rates of phosphate dissociation to be different than the model predications where ATP hydrolysis is not occurring. This allowed for the conclusion that the main influence of the thin filament is to determine the rate of phosphate dissociation and that regulation is dependent on the ligands associated with these thin filaments.

Another recent study, titled “Intrinsic dynamic behavior of fascin in filopodia” was published in 2007 and presented experimental and computational methods as an approach to determine features of fascin exchange and incorporation in filopodia. Fascin is an actin cross linking protein found between filopodial filaments. This study determined that phosphorylated fascin is freely diffusing, in contrast to actin bundling that’s primary achieved by dephosphorylated fascin.  Using florescence recovery after photobleaching, results show that fascin is rapidly dissociated from filopodial filaments and undergoes diffusion. Reversible cross- linking is necessary for the delivery of fascin to growing filopodial tips according to the derived computational model. Analysis of the fascin bundling shows that filopodia are made of bundles with one fascin per roughly 25-60 actin monomers. Overall, this study gave insight into fascin behavior and its role in growing filopodia.

Taylor also highlights his research interests in  another 2007 article titled “Self-organization of actin filament orientation in the dendritic-nucleation/array-treadmilling model.” Presented here is a dendritic-nucleation/array-treadmilling model that provides a framework for synthesis of the action network in motile cells. Using lamellipodia, a 2D stochastic computer model was used to study the organization of filaments and their associated orientations. Model parameters were input using estimates from literature, which provided necessary values for the leading edge-branching/capping-protective zone and the autocatalytic branch rate. The parameters set resulted in a preference for +/- 35 degree filaments shown in lamellipodial electron micrographs. This organization requires 12 generations of branching to cause a 15 degree change in movement direction, as well as protection from capping at the leading edge and a minimum of 60 degrees for individual branching angles. Overall, they discovered a +/- 70 degree pattern in flexible filaments. This study provided insight into actin treadmilling and its associated branching, a concept critical to the movement of lamellipodia.

Awards and Memberships

Edwin Taylor was awarded the E.B Wilson Medal in 1999, which is the ASCB’s highest honor for science and presented to those who contribute to the field of cell biology over their lifetime. He was also accepted into the National Academy of Sciences in 2001. Other memberships include the Royal Society of London and the American Academy of Arts and Sciences.

Grants and Funding

In 1989, Edwin Taylor received a research grant from the National Institute of General Medical Sciences while working at the University of Chicago in the School of Medicine. The grant supported research in Cellular and Molecular Basis of Disease.

From 1995 to 1998, Edwin Taylor received another NIH grant to fund his research on the mechanisms of motor protein synthesis. At this time, he was still at The University of Chicago in the School of Medicine.

External links

• https://www.youtube.com/watch?v=FnqY6FF2wWI&t=181s