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

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Bakthavatsalam D,Soung RH,Tweardy DJ,Chiu W,Dixon RA,Woodside DG

doi

10.1016/j.febslet.2014.04.049

subject

Has Abstract

pub_date

2014-06-13 00:00:00

pages

2133-40

issue

13

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(14)00372-X

journal_volume

588

pub_type

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