The Ankrd13 Family of Ubiquitin-interacting Motif-bearing Proteins Regulates Valosin-containing Protein/p97 Protein-mediated Lysosomal Trafficking of Caveolin 1.

The Journal of Biological Chemistry
Daocharad BuranaMasayuki Komada

Abstract

Caveolin 1 (Cav-1) is an oligomeric protein that forms flask-shaped, lipid-rich pits, termed caveolae, on the plasma membrane. Cav-1 is targeted for lysosomal degradation in ubiquitination- and valosin-containing protein (VCP)-dependent manners. VCP, an ATPase associated with diverse cellular activities that remodels or segregates ubiquitinated protein complexes, has been proposed to disassemble Cav-1 oligomers on the endosomal membrane, facilitating the trafficking of Cav-1 to the lysosome. Genetic mutations in VCP compromise the lysosomal trafficking of Cav-1, leading to a disease called inclusion body myopathy with Paget disease of bone and/or frontotemporal dementia (IBMPFD). Here we identified the Ankrd13 family of ubiquitin-interacting motif (UIM)-containing proteins as novel VCP-interacting molecules on the endosome. Ankrd13 proteins formed a ternary complex with VCP and Cav-1 and exhibited high binding affinity for ubiquitinated Cav-1 oligomers in an UIM-dependent manner. Mass spectrometric analyses revealed that Cav-1 undergoes Lys-63-linked polyubiquitination, which serves as a lysosomal trafficking signal, and that the UIMs of Ankrd13 proteins bind preferentially to this ubiquitin chain type. The overexpression of An...Continue Reading

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Citations

Jul 23, 2016·Frontiers in Cell and Developmental Biology·Bing HanAnne K Kenworthy
Jan 27, 2017·American Journal of Physiology. Cell Physiology·Anna R BusijaPaul A Insel
Aug 19, 2017·The Biochemical Journal·Lasse Stach, Paul S Freemont
Jul 1, 2018·Neural Development·Vladimir Vladimirovich MuzykaTudor Constantin Badea
Aug 1, 2019·Biomolecules·America CamposAndrew Frederick Geoffery Quest

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