Chaperonin-containing TCP-1 complex directly binds to the cytoplasmic domain of the LOX-1 receptor |
| |
| Authors: | Deenadayalan Bakthavatsalam Roh Hun Soung David J. Tweardy Wah Chiu Richard A.F. Dixon Darren G. Woodside |
| |
| Affiliation: | 1. Department of Molecular Cardiology, Texas Heart Institute, Houston, TX 77030, USA;2. National Center for Macromolecular Imaging, Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA;3. Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA |
| |
| Abstract: | Lectin-like oxidized low-density lipoprotein receptor (LOX-1) is a scavenger receptor that binds oxidized low-density lipoprotein (OxLDL) and has a role in atherosclerosis development. The N-terminus intracellular region (cytoplasmic domain) of LOX-1 mediates receptor internalization and trafficking, potentially through intracellular protein interactions. Using affinity isolation, we identified 6 of the 8 components of the chaperonin-containing TCP-1 (CCT) complex bound to LOX-1 cytoplasmic domain, which we verified by coimmunoprecipitation and immunostaining in human umbilical vein endothelial cells. We found that the interaction between CCT and LOX-1 is direct and ATP-dependent and that OxLDL suppressed this interaction. Understanding the association between LOX-1 and the CCT complex may facilitate the design of novel therapies for cardiovascular disease. |
| |
| Keywords: | CCT complex Lectin-like oxidized low-density lipoprotein receptor Atherosclerosis Protein&ndash protein interaction |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
