An intracellular traffic jam: Fc receptor-mediated transport of immunoglobulin G
- Creators
- Tesar, Devin B.
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Bjorkman, Pamela J.
Abstract
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.
Additional Information
© 2010 Elsevier. Available online 18 February 2010. We thank Marta Murphy and Ron Diskin for help making figures. Studies of FcRn are supported in PJB's laboratory by the National Institutes of Health (2 R37 AI041239-06A1). DBT is a full-time employee of Genentech, Inc.Attached Files
Accepted Version - nihms198415.pdf
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Additional details
- PMCID
- PMC2865255
- Eprint ID
- 18608
- DOI
- 10.1016/j.sbi.2010.01.010
- Resolver ID
- CaltechAUTHORS:20100609-080121667
- NIH
- 2 R37 AI041239-06A1
- Created
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2010-06-09Created from EPrint's datestamp field
- Updated
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2021-11-08Created from EPrint's last_modified field