We use cookies to understand how you use our site and to improve your experience. This includes personalizing content and advertising. To learn more, click here. By continuing to use our site, you accept our use of cookies. Cookie Policy.

Features Partner Sites Information LinkXpress hp
Sign In
Advertise with Us

Download Mobile App




Novel Enzyme Binding Mechanism Dooms LDL-Receptors

By LabMedica International staff writers
Posted on 27 Dec 2011
Cardiovascular disease researchers have described the mode of action of an enzyme that regulates levels of low-density lipoprotein (LDL)-cholesterol by marking LDL-receptors for degradation by the cell’s protein recycling mechanism.

Cells in the liver produce LDL-receptors that bind LDL and remove it from the blood, thereby lowering cholesterol levels. More...
The E3 ubiquitin ligase IDOL (inducible degrader of the LDL receptor) is one of the enzymes involved in this process. By causing the destruction of LDL-receptors this enzyme slows the removal of LDL and increases the amount of cholesterol in circulation.

In the current study, investigators at the University of Leicester (United Kingdom) and the University of California Los Angeles (USA) traced the molecular pathway used by IDOL to mark LDL-receptors for destruction.

They reported in the November 22, 2011, online edition of the journal Proceedings of the [US] National Academy of Sciences (PNAS) that IDOL used a singular strategy among E3 ligases for target recognition. The IDOL FERM domain bound directly to a recognition sequence in the cytoplasmic tails of lipoprotein receptors. The FERM domain (F for 4.1 protein, E for ezrin, R for radixin, and M for moesin) is a widespread protein module involved in localizing proteins to the plasma membrane. FERM domains are found in a number of cytoskeletal-associated proteins that associate with various proteins at the interface between the plasma membrane and the cytoskeleton. The FERM domain is located at the N terminus of the majority of FERM-containing proteins.

Target recognition by IDOL involved a tripartite interaction between the FERM domain, membrane phospholipids, and the lipoprotein receptor tail. This physical interaction was independent of IDOL’s gene (RING) domain E3 ligase activity and its capacity for autoubiquitination. Furthermore, IDOL controlled its own stability through autoubiquitination of a unique FERM subdomain fold not present in other FERM proteins.

Contributing author Dr. John Schwabe, professor of biochemistry at the University of Leicester, said, “Remarkably, IDOL only targets three proteins for degradation (all lipoprotein receptors) and this research paper greatly enhances our understanding of this specificity and identifies key residues involved in mediating this interaction. Development of a drug that interferes with IDOL's activity could help lower levels of LDL. Our research has greatly enhanced our understanding of this important process. A potential future drug that targets IDOL could be prescribed in conjunction with statin drugs, which also cut cholesterol levels by increasing production of the LDL receptor and this study makes considerable headway towards this.”

Related Links:

University of Leicester
University of California Los Angeles



Gold Member
Quantitative POC Immunoassay Analyzer
EASY READER+
POC Helicobacter Pylori Test Kit
Hepy Urease Test
New
Pipette
Accumax Smart Series
New
Human Estradiol Assay
Human Estradiol CLIA Kit
Read the full article by registering today, it's FREE! It's Free!
Register now for FREE to LabMedica.com and get access to news and events that shape the world of Clinical Laboratory Medicine.
  • Free digital version edition of LabMedica International sent by email on regular basis
  • Free print version of LabMedica International magazine (available only outside USA and Canada).
  • Free and unlimited access to back issues of LabMedica International in digital format
  • Free LabMedica International Newsletter sent every week containing the latest news
  • Free breaking news sent via email
  • Free access to Events Calendar
  • Free access to LinkXpress new product services
  • REGISTRATION IS FREE AND EASY!
Click here to Register








Channels

Molecular Diagnostics

view channel
Image: Researchers identified SARS-CoV-2 protein fragments within extracellular vesicles in the blood of long COVID patients (Photo courtesy of Shutterstock)

Blood Biomarker Test Could Confirm Long COVID Diagnosis

Long COVID remains a diagnostic challenge, with clinicians currently relying on a collection of symptoms that appear 12 weeks or more after SARS-CoV-2 infection. No blood tests or biomarkers currently... Read more

Hematology

view channel
Image: The microfluidic device for passive separation of platelet-rich plasma from whole blood (Photo courtesy of University of the Basque Country)

Portable and Disposable Device Obtains Platelet-Rich Plasma Without Complex Equipment

Platelet-rich plasma (PRP) plays a crucial role in regenerative medicine due to its ability to accelerate healing and repair tissue. However, obtaining PRP traditionally requires expensive centrifugation... Read more

Immunology

view channel
Image: Insights into sarcomatoid renal cell carcinoma point to broader use of common immunotherapies (Photo courtesy of Salgia NJ et al., Cancer Cell, 2025)

Novel Gene Signature Predicts Immunotherapy Response in Advanced Kidney Cancers

Sarcomatoid renal cell carcinoma (sRCC) is a rare, aggressive form of kidney cancer comprising about 5% of cases and is typically diagnosed at late stages. Resistant to most therapies, it has shown unusually... Read more
Copyright © 2000-2025 Globetech Media. All rights reserved.