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A more recent version of this article appeared on September 1, 2004
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Submitted on March 23, 2004
Revised on June 15, 2004
Accepted on June 16, 2004
Receptor Recycling Regulated by Clathrin-mediated Endocytosis and Rab11
Thoracic Diseases Research Unit, Department of Biochemistry and Molecular Biology and Mayo Clinic Cancer Center, Mayo Clinic, Rochester, MN 55905
Monitoring Editor: Carl-Henrik Heldin
Proteins in the transforming growth factor-
(TGF-) family recognize transmembrane serine/threonine kinases known as type I and type II receptors. Binding of TGF- to receptors results in receptor down-regulation and signaling. While previous work has focused on activities controlling TGF- signaling, more recent studies have begun to address the trafficking properties of TGF- receptors. In this report it is shown that receptors undergo recycling both in the presence and absence of ligand activation, with the rates of internalization and recycling being unaffected by ligand binding. Recycling occurs as receptors are most likely internalized through clathrin-coated pits, then returned to the plasma membrane via a rab11-dependent, rab4-independent mechanism. The data suggest that raft/caveolae-dependent endocytosis is of minor importance, although its involvement in the endocytosis of TGF- receptors cannot be formally ruled out. Taken together, the results suggest a mechanism wherein activated TGF- receptors are directed to a distinct endocytic pathway for down-regulation and degradation following one or more rounds of recycling.
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