Work

Chaperonin‐containing TCP‐1 complex directly binds to the cytoplasmic domain of the LOX‐1 receptor

Year: 2014

Type: article

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.

Source: FEBS Letters

DOI: 10.1016/j.febslet.2014.04.049

Authors: Deenadayalan Bakthavatsalam, Roh Hun Soung, David J. Tweardy, Wah Chiu, Richard A.F. Dixon, Darren G. Woodside

Institution: Baylor College of Medicine

Language: English

Topic: Atherosclerosis and Cardiovascular Diseases

Subfield: Immunology

Field: Immunology and Microbiology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: bronze