May 8, 2019
Michael McMurray featured in Biochemistry and Molecular Biophysics Seminar today
Submitted by Biochemistry and Molecular Biophysics
Michael McMurray, associate professor of cell and developmental biology at the University of Colorado, Anschutz Medical Campus, is the featured speaker for Biochemistry and Molecular Biophysics Seminar on Wednesday, May 8. He will present "It's not the destination, it's the journey: septin protein complexes as a model to understand multisubunit assembly in vivo" at 4 p.m. in 120 Ackert Hall.
McMurray earned his Bachelor of Science in biochemistry and genetics at Texas A&M University. He performed his doctoral research in the lab of Dan Gottschling at the Fred Hutchinson Cancer Research Center in Seattle and received the Harold M. Weintraub award for outstanding achievement during graduate studies in the biological sciences. His postdoctoral research was conducted in the lab of Jeremy Thorner at the University of California, Berkeley, supported in part by a fellowship from the Jane Coffin Childs Memorial Fund for Medical Research, and a K99/R00 Pathway to Independence Award from the NIH. In 2011 McMurray started his own lab in the department of cell and developmental biology at the University of Colorado School of Medicine, where he was promoted to associate professor in 2018.
Cellular function requires the assembly of macromolecular complexes composed of distinct polypeptide subunits that interact in precise ways. Protein sequence is often not enough to guarantee that in the crowded cellular environment each nascent subunit makes only the correct protein-protein interactions. Incorrect conformations and interactions lead to cellular defects, and human disease. How cells ensure that newly-synthesized polypeptides assemble into functional complexes remains poorly understood. Septin proteins assemble into highly conserved cytoskeletal hetero-oligomers that have emerged as central players in many cellular processes. All septin subunits are structurally related, yet the organization of hetero-oligomers is tightly controlled by mechanisms that remain unclear. Mutations that affect septin protein folding cause male infertility, and misfolding of wildtype septins may contribute to other diseases — e.g. Alzheimer's. Molecular chaperones promote the proper folding and assembly of many proteins, but it is not known if septins are among them. In the McMurray lab, we use a yeast system and imaging, biochemical, and genetic approaches to understand the molecular requirements for proper de novo assembly of septin hetero-oligomers.