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Vol. 16, Issue 5, 2470-2482, May 2005
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* Department of Neurobiology and Anatomy, University of Texas Medical School, Houston, TX 77030;
Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands; and
Department of Microbiology and Molecular Genetics, University of Texas Medical School, Houston, TX 77030
Submitted November 19, 2004;
Accepted March 2, 2005
Monitoring Editor: Howard Riezman
Altering the number of surface receptors can rapidly modulate cellular responses to extracellular signals. Some receptors, like the transferrin receptor (TfR), are constitutively internalized and recycled to the plasma membrane. Other receptors, like the epidermal growth factor receptor (EGFR), are internalized after ligand binding and then ultimately degraded in the lysosome. Routing internalized receptors to different destinations suggests that distinct molecular mechanisms may direct their movement. Here, we report that the endosome-associated protein hrs is a subunit of a protein complex containing actinin-4, BERP, and myosin V that is necessary for efficient TfR recycling but not for EGFR degradation. The hrs/actinin-4/BERP/myosin V (CART [cytoskeleton-associated recycling or transport]) complex assembles in a linear manner and interrupting binding of any member to its neighbor produces an inhibition of transferrin recycling rate. Disrupting the CART complex results in shunting receptors to a slower recycling pathway that involves the recycling endosome. The novel CART complex may provide a molecular mechanism for the actin-dependence of rapid recycling of constitutively recycled plasma membrane receptors.
Abbreviations used: CART, cytoskeleton-associated recycling or transport; EGF, epidermal growth factor; Hrs, hepatocyte growth factor stimulated serum phosphoprotein; Tf, transferrin.
Address correspondence to: Andrew Bean (a.bean{at}uth.tmc.edu).
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