Nav: Home

The molecular mechanism that blocks membrane receptors has been identified

October 26, 2016

The study began by taking the medical history of 11 children, all of whom had a disorder due to mycobacteria infections, as the basis. All were discovered to have the same phenotype with the same mutation, which was located in the interferon-gamma (IFNGR) receptor, so the group began to explore what was causing this dysfunction.

The cell membrane can be likened to an ocean, a sea consisting mainly of lipids and proteins, in which there are islands made up of specific lipids such as cholesterol and sphingolipids. The membrane proteins are located on the islands and can only perform their function in these nanodomains.

The IFNGR receptor is one of these membrane proteins and undertakes to activate genes involved in a huge variety of cell processes, including defence against pathogens and cancer. The team discovered that a simple mutation in the chain of 337 aminoacids that form it allows a sugar to be added. This sugar is recognised by a protein in the family of extracellular proteins known as galectins. When that protein is added to the receptor, the receptor gets taken out of its nanodomain and becomes caught up in the actin filaments that form the cell's cytoskeleton. Once outside its nanodomain, the receptor becomes blocked and can no longer transmit the signal.

"The research provides direct evidence on the fundamental role that certain lipid nanodomains play in the activation and regulation of cell signalling mediated by the IFNGR receptor. What is more, the results of this work stress the need to study the interaction between galectins and highly glycosylated membrane receptors and the link with various congenital diseases," pointed out Xabier Contreras. The study is also offering possible therapeutic targets for treating patients who are carriers of the IFNGR receptor mutation.
-end-
Bibliographical reference

Blouin CM, Hamon Y, Gonnord P, Boularan C, Kagan J, Viaris de Lesegno C, Ruez R, Mailfert S, Bertaux N, Loew D, Wunder C, Johannes L, Vogt G, Contreras FX, Marguet D, Casanova JL, Galès C, He HT, Lamaze C Glycosylation-Dependent IFN-γR Partitioning in Lipid and Actin Nanodomains is Critical for JAK Activation. Cell. 2016 Aug 11;166(4):920-34. doi: 10.1016/j.cell.2016.07.003

University of the Basque Country

Related Proteins Articles:

Designing vaccines from artificial proteins
EPFL scientists have developed a new computational approach to create artificial proteins, which showed promising results in vivo as functional vaccines.
New method to monitor Alzheimer's proteins
IBS-CINAP research team has reported a new method to identify the aggregation state of amyloid beta (Aβ) proteins in solution.
Composing new proteins with artificial intelligence
Scientists have long studied how to improve proteins or design new ones.
Hero proteins are here to save other proteins
Researchers at the University of Tokyo have discovered a new group of proteins, remarkable for their unusual shape and abilities to protect against protein clumps associated with neurodegenerative diseases in lab experiments.
Designer proteins
David Baker, Professor of Biochemistry at the University of Washington to speak at the AAAS 2020 session, 'Synthetic Biology: Digital Design of Living Systems.' Prof.
Gone fishin' -- for proteins
Casting lines into human cells to snag proteins, a team of Montreal researchers has solved a 20-year-old mystery of cell biology.
Coupled proteins
Researchers from Heidelberg University and Sendai University in Japan used new biotechnological methods to study how human cells react to and further process external signals.
Understanding the power of honey through its proteins
Honey is a culinary staple that can be found in kitchens around the world.
How proteins become embedded in a cell membrane
Many proteins with important biological functions are embedded in a biomembrane in the cells of humans and other living organisms.
Finding the proteins that unpack DNA
A new method allows researchers to systematically identify specialized proteins called 'nuclesome displacing factors' that unpack DNA inside the nucleus of a cell, making the usually dense DNA more accessible for gene expression and other functions.
More Proteins News and Proteins Current Events

Trending Science News

Current Coronavirus (COVID-19) News

Top Science Podcasts

We have hand picked the top science podcasts of 2020.
Now Playing: TED Radio Hour

Making Amends
What makes a true apology? What does it mean to make amends for past mistakes? This hour, TED speakers explore how repairing the wrongs of the past is the first step toward healing for the future. Guests include historian and preservationist Brent Leggs, law professor Martha Minow, librarian Dawn Wacek, and playwright V (formerly Eve Ensler).
Now Playing: Science for the People

#566 Is Your Gut Leaking?
This week we're busting the human gut wide open with Dr. Alessio Fasano from the Center for Celiac Research and Treatment at Massachusetts General Hospital. Join host Anika Hazra for our discussion separating fact from fiction on the controversial topic of leaky gut syndrome. We cover everything from what causes a leaky gut to interpreting the results of a gut microbiome test! Related links: Center for Celiac Research and Treatment website and their YouTube channel
Now Playing: Radiolab

The Flag and the Fury
How do you actually make change in the world? For 126 years, Mississippi has had the Confederate battle flag on their state flag, and they were the last state in the nation where that emblem remained "officially" flying.  A few days ago, that flag came down. A few days before that, it coming down would have seemed impossible. We dive into the story behind this de-flagging: a journey involving a clash of histories, designs, families, and even cheerleading. This show is a collaboration with OSM Audio. Kiese Laymon's memoir Heavy is here. And the Hospitality Flag webpage is here.