An intracellular traffic jam: Fc receptor-mediated transport of immunoglobulin G.
Recent advances in imaging techniques along with more powerful in vitro and in vivo models of receptor-mediated ligand transport are facilitating advances in our understanding of how cells efficiently direct receptors and their cargo to target destinations within the cytoplasm and at the plasma membrane. Specifically, light and 3D electron microscopy studies examining the trafficking behavior of the neonatal Fc receptor (FcRn), a transport receptor for immunoglobulin G (IgG), have given us new insights into the dynamic interplay between the structural components of the cytosolic trafficking machinery, its protein regulators, and the receptors it directs to various locations within the cell. These studies build upon previous biochemical characterizations of FcRn transport and are allowing us to begin formulation of a more complete model for the intracellular trafficking of receptor-ligand complexes.
Tesar
Devin B
DB
Department of Antibody Engineering, Genentech, South San Francisco, CA 94080, USA. devint@gene.com
Björkman
Pamela J
PJ
D000595:Amino Acid Sequence; D000818:Animals; D001692:Biological Transport; D006801:Humans; D007074:Immunoglobulin G / Q000378:metabolism*; D008954:Models, Biological; D008969:Molecular Sequence Data; D011961:Receptors, Fc / Q000378:metabolism*
D007074:Immunoglobulin G; D011961:Receptors, Fc