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Chaperonin‐containing TCP‐1 complex directly binds to the cytoplasmic domain of the LOX‐1 receptor
Author(s) -
Bakthavatsalam Deenadayalan,
Soung Roh Hun,
Tweardy David J.,
Chiu Wah,
Dixon Richard A.F.,
Woodside Darren G.
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.04.049
Subject(s) - chaperonin , scavenger receptor , internalization , cytoplasm , microbiology and biotechnology , receptor , immunoprecipitation , intracellular , umbilical vein , chemistry , ldl receptor , biochemistry , lipoprotein , biophysics , biology , cholesterol , protein folding , gene , in vitro
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.