The formin family of cytoskeletal remodeling proteins are lauded for thier performances at numerous biological venues. Typically acting as effectors for Rho family GTP-binding proteins, formins were shown to be crucial in cell motility and division. Later, formins achieved celebrity status when they demonstrated direct participation in actin filament assembly. Following that performance, their fame has become widespread. Most reviews on formins have emphasized the many outstanding biochemical and structural studies describing how formins nucleate, processively elongate, and in some cases bundle non-branched actin filaments. This special issue on formins spotlights new roles in cell morphology and cell signaling networks influencing development and growth control.
Art Alberts, Ph.D., is a Distinguished Scientific Investigator at the Van Andel Institute (VAI), Grand Rapids, Michigan. Dr. Alberts received his B.A. in biochemistry and cell biology in 1987 and his Ph.D. in physiology and pharmacology in 1993 at the University of California, San Diego. He was a post-doctoral Fellow in the Transcription Laboratory at the Imperial Cancer Research Fund, Lincoln's Inn Fields (now the London Research Institute of Cancer Research UK) from 1994 to 1997. There, he studied signaling pathways regulated by Rho family small GTP-binding proteins with Dr. Richard Treisman. He was an Assistant Research Biochemist and a Carol Franc Buck Fellow at the University of California, San Francisco in the laboratory of Dr. Frank McCormick until 2000 when he joined the Van Andel Institute as a Principal Investigator. Current research in the lab focuses on the spatial and temporal regulation of cell signaling networks that govern cell growth and differentiation. He has been the Director of the VAI Flow Cytometry Facility since 2006. Dr. Alberts is currently a Distinguished Investigator and holds adjunct appointments in the Department of Genetics and the Cell and Molecular Biology Program at Michigan State University.
BBA - Molecular Cell Research
