Cellular and Molecular Life Sciences CMLS

, Volume 61, Issue 19, pp 2461–2470

Low-density lipoprotein receptor structure and folding

Review

DOI: 10.1007/s00018-004-4090-3

Cite this article as:
Gent, J. & Braakman, I. CMLS, Cell. Mol. Life Sci. (2004) 61: 2461. doi:10.1007/s00018-004-4090-3

Abstract.

The endoplasmic reticulum (ER) is a major cellular ‘production factory’ for many membrane and soluble proteins. A quality control system ensures that only correctly folded and assembled proteins leave the compartment. The low-density lipoprotein receptor (LDLR) is the prototype of a large family of structurally homologous cell surface receptors, which fold in the ER and function as endocytic and signaling receptors in a wide variety of cellular processes. Patients with familial hypercholesterolemia carry single or multiple mutations in their LDLR, which leads to malfunction of the protein, in most patients through misfolding of the receptor. As a result, clearance of cholesterol-rich LDL particles from the circulation decreases, and the elevated blood cholesterol levels cause early onset of atherosclerosis and an increased risk of cardiac disease in these patients. In this review, we will elaborate on the structural aspects of the LDLR and its folding pathway and compare it to other LDLR family members.

Key words.

LDL receptorstructurefoldingchaperonesdisulfide bonds

Copyright information

© Birkhäuser Verlag, Basel 2004

Authors and Affiliations

  1. 1.Department of Bio-organic Chemistry 1Utrecht UniversityCH UtrechtThe Netherlands