NHERF1 and NHERF2 regulation of SR-B1 stability via ubiquitination and proteasome degradation.
Biochem Biophys Res Commun
; 490(4): 1168-1175, 2017 09 02.
Article
in En
| MEDLINE
| ID: mdl-28669731
ABSTRACT
Scavenger receptor class B type 1 (SR-B1), an HDL receptor plays a crucial role in cholesterol metabolism in the liver, steroidogenic tissues, and vascular cells including macrophages. SR-B1 is subject to regulation at the transcription, posttranscription and posttranslational levels. We previously provided evidence that PDZ domain containing NHERF1 and NHERF2 regulate SR-B1 protein levels post-transcriptionally, although the underlying mechanism(s) by which NHERF1 and NHERF2 regulate SR-B1 protein levels is not well understood. In this study, we demonstrate that SR-B1 is degraded intracellularly via ubiquitin-proteasome pathway and that SR-B1 can be ubiquitinated at K500 and K508 residues. Overexpression of NHERF1 or NHERF2 enhanced SR-B1 ubiquitination and degradation. NHERF1 and NHERF2 promote SR-B1 ubiquitination at sites K508 and K500, respectively. These results suggest that NHERF1 and NHERF2 down-regulated SR-B1 at least in part via the ubiquitin/proteasome pathway.
Key words
Full text:
1
Database:
MEDLINE
Main subject:
Phosphoproteins
/
Sodium-Hydrogen Exchangers
/
Proteasome Endopeptidase Complex
/
Scavenger Receptors, Class B
Limits:
Animals
Language:
En
Year:
2017
Type:
Article