The recycling and transcytotic pathways for IgG transport by FcRn are distinct and display an inherent polarity
| Autor: | Steen H. Hansen, Salit Tzaban, Wendy Hamman, Richard S. Blumberg, Scott R. Frank, Lynne A. Lapierre, Ramiro Massol, James R. Goldenring, Wayne I. Lencer, Elizabeth H. Yen |
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| Jazyk: | angličtina |
| Rok vydání: | 2009 |
| Předmět: |
Endosome
Myosin Type V Fc receptor Endosomes Receptors Fc Biology Article Cell Line Cell membrane 03 medical and health sciences 0302 clinical medicine Dogs Cell polarity medicine Animals Humans Research Articles 030304 developmental biology Epithelial polarity 0303 health sciences Myosin Heavy Chains Cell Membrane Cell Polarity Cell Biology Cell biology Transport protein Cell Compartmentation Protein Transport medicine.anatomical_structure Transcytosis rab GTP-Binding Proteins 030220 oncology & carcinogenesis Immunoglobulin G biology.protein RAB11A |
| Zdroj: | The Journal of Cell Biology |
| ISSN: | 1540-8140 0021-9525 |
| Popis: | The Fc receptor FcRn traffics immunoglobulin G (IgG) in both directions across polarized epithelial cells that line mucosal surfaces, contributing to host defense. We show that FcRn traffics IgG from either apical or basolateral membranes into the recycling endosome (RE), after which the actin motor myosin Vb and the GTPase Rab25 regulate a sorting step that specifies transcytosis without affecting recycling. Another regulatory component of the RE, Rab11a, is dispensable for transcytosis, but regulates recycling to the basolateral membrane only. None of these proteins affect FcRn trafficking away from lysosomes. Thus, FcRn transcytotic and recycling sorting steps are distinct. These results are consistent with a single structurally and functionally heterogeneous RE compartment that traffics FcRn to both cell surfaces while discriminating between recycling and transcytosis pathways polarized in their direction of transport. |
| Databáze: | OpenAIRE |
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