The FG phase and transport selectivity through nuclear pores

Dr. Dirk Görlich studied biochemistry at the Martin Luther University in Halle (Germany). For his Ph.D., he joined Tom Rapoport’s lab in Berlin, where he identified the heterotrimeric Sec61αβγ complex as a receptor for translating ribosomes and the protein-conducting channel of the endoplasmic reticulum (ER). He also succeeded in reconstituting a fully functional “translocon” from purified components and demonstrated its capacity to transport secretory proteins across the ER membrane and to integrate type I and type II membrane proteins into the lipid bilayer. 1994, he joined Ron Laskey’s lab in Cambridge, where he discovered the first importins as mediators of protein import into the cell nucleus. In 1996, he became an independent group leader and later a professor for molecular biology at the ZMBH (University of Heidelberg). During this time, he put forward the RanGTP-gradient model to explain the directionality and energetics of nuclear transport, and his group was instrumental in discovering and characterising exportins, which mediate export from the cell nucleus. He is now a director at the Max Planck Institute for Multidisciplinary Sciences in Göttingen and focused on the question of how nuclear pore complexes function as highly efficient transport machines. His team discovered that intrinsically disordered FG domains assemble into a condensed (selective) phase that functions as a highly selective permeability barrier of extreme transport capacity. His group also develops nanobodies as cell biological tools and as therapeutics for treating viral infections, bacterial sepsis, and autoimmune conditions. He received the EMBO Gold Medal, the WLA prize as well as the Louis-Jeantet Prize.