KIF13B enhances the endocytosis of LRP1 by recruiting LRP1 to caveolae
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منابع مشابه
KIF13B enhances the endocytosis of LRP1 by recruiting LRP1 to caveolae
Multifunctional low-density lipoprotein (LDL) receptor-related protein 1 (LRP1) recognizes and internalizes a large number of diverse ligands, including LDL and factor VIII. However, little is known about the regulation of LRP1 endocytosis. Here, we show that a microtubule-based motor protein, KIF13B, in an unexpected and unconventional function, enhances caveolin-dependent endocytosis of LRP1....
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M icrotubule-based kinesin motor proteins have many cellular functions, including the transport of various cargoes to different parts of the cell (1). Kanai et al. uncover an unexpected , motor-independent function for one kinesin, KIF13B, in promoting the endocy-tosis of a membrane receptor that regulates cholesterol levels in the blood (2). There are 45 kinesins in the human genome, and the f...
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The relationship between low-density lipoprotein receptor-related protein-1 (LRP1) and von Willebrand factor (VWF) has remained elusive for years. Indeed, despite a reported absence of interaction between both proteins, liver-specific deletion of LRP1 results in increased VWF levels. To investigate this discrepancy, we used mice with a macrophage-specific deficiency of LRP1 (macLRP1(-)) because...
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OBJECTIVE The purpose of this study was to determine the significance of the intracellular NPxYxxL motif of LRP1 for the atheroprotective role of this multifunctional receptor. METHODS AND RESULTS LRP1 knock-in mice carrying an inactivating mutation in the NPxYxxL motif were crossed with LDLR-deficient mice, a model for atherosclerosis. In this LDLR(-/-) background the mutated mice showed a m...
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ژورنال
عنوان ژورنال: Journal of Cell Biology
سال: 2014
ISSN: 1540-8140,0021-9525
DOI: 10.1083/jcb.201309066