Navigation Links
MDC researchers identify a scaffold regulating protein disposal
Date:12/11/2009

How does a cell manage to identify and degrade the diverse types of defective proteins and thus protect the body against serious diseases? The researchers Sabine C. Horn, Professor Thomas Sommer, Professor Udo Heinemann and Dr. Ernst Jarosch of the Max Delbrck Center for Molecular Medicine (MDC) Berlin-Buch, Germany, have now found a crucial piece in this puzzle. In an enzyme complex that plays a critical role in the quality control of proteins, they discovered a scaffold regulating the identification and disposal of various defectively produced proteins. (Molecular Cell, doi: 10.1016/j.molcel200910.015)*.

Proteins are the building materials and the machinery of life. They are found by the thousands in a cell and carry out vital tasks in the organism.

The production site of many of the proteins is located in a cell organelle called the endoplasmic reticulum (ER). Here the proteins are produced, folded and routed to their destination.

However, during protein production errors can occur: during the process proteins can be folded in the wrong way. Older proteins may also accumulate defects due to environmental stress.

They can lose their original structure and thus fail to carry out their function and may possibly even cause damage. Diseases can develop such as Alzheimer's, Parkinson's or cystic fibrosis. Defective proteins must therefore be detected in the cell and disposed of.

Protein quality control: rejects receive a molecular tag

Proteins run through a quality control process in the cell. For the identification of defective proteins, an enzyme complex the HRD-ubiquitin ligase plays a key role.

It functions like a kind of tagging machine: If it recognizes the protein as defective, it tags it with a molecule, the protein ubiquitin, thus marking it for disposal.

Great demands are placed on the HRD-ubiquitin ligase, because proteins adapt to their cellular locations and functions and thus have quite different structures.

For instance, there are water-soluble proteins inside the cell as well as water-insoluble proteins that are situated on or in the cell membrane.

Until now it remained unclear how the enzyme complex manages to recognize and mark such different types of proteins.

Flexible scaffold makes tagging machine universally usable

The study of the MDC researchers has now shed light on this puzzle. The researchers have discovered the central and flexible scaffold of the enzyme complex, the subunit Usa1. Depending on what is required, it tethers specific modules of the complex, connecting them with each other.

When identifying and tagging soluble proteins, Usa1 establishes the contact between the subunits Der1 and Hrd1.

Furthermore, the researchers discovered that the HRD-ubiquitin ligase binds with other HRD-ubiquitin ligases to form a larger enzyme complex in order to degrade insoluble membrane proteins. This process is also regulated by the subunit Usa1.


'/>"/>

Contact: Barbara Bachtler
bachtler@mdc-berlin.de
49-309-406-3896
Helmholtz Association of German Research Centres
Source:Eurekalert

Related biology news :

1. UCLA researchers engineer bacteria to turn carbon dioxide into liquid fuel
2. Berkeley Lab researchers participate in Homeland Security study of subway airflow
3. Hebrew University, American researchers show trigger to stem cell differentiation
4. Carnegie Mellon researchers receive grant
5. Researchers finds hidden sensory system in the skin
6. Researchers demonstrate nanoscale X-ray imaging of bacterial cells
7. Texas AgriLife researchers helping
8. Stopping MRSA before it becomes dangerous is possible, Sandia/UNM researchers find
9. VAI researchers find long awaited key to creating drought resistant crops
10. UGA researchers lead team in discovery involving devastating freshwater fish parasite, Ich
11. Nervy research: Researchers take initial look at ion channels in a model system
Post Your Comments:
*Name:
*Comment:
*Email:
(Date:4/13/2017)... According to a new market research report "Consumer IAM Market ... Authorization), Service, Authentication Type, Deployment Mode, Vertical, and Region - Global Forecast ... from USD 14.30 Billion in 2017 to USD 31.75 Billion by 2022, ... ... MarketsandMarkets Logo ...
(Date:4/11/2017)... April 11, 2017 No two people ... at the New York University Tandon School of ... have found that partial similarities between prints are ... in mobile phones and other electronic devices can ... The vulnerability lies in the fact that fingerprint-based ...
(Date:4/5/2017)... Allen Institute for Cell Science today announces the launch ... dynamic digital window into the human cell. The website ... deep learning to create predictive models of cell organization, ... suite of powerful tools. The Allen Cell Explorer will ... resources created and shared by the Allen Institute for ...
Breaking Biology News(10 mins):
(Date:10/11/2017)... Oct. 11, 2017  VMS BioMarketing, a leading provider of ... oncology Clinical Nurse Educator (CNE) network, which will launch this ... communication among health care professionals to enhance the patient care ... staff, and other health care professionals to help women who ... ...
(Date:10/11/2017)... ... October 11, 2017 , ... Singh Biotechnology ... drug designation to SBT-100, its novel anti-STAT3 (Signal Transducer and Activator of Transcription ... is able to cross the cell membrane and bind intracellular STAT3 and inhibit ...
(Date:10/10/2017)... ... 10, 2017 , ... Dr. Bob Harman, founder and CEO of VetStem ... The event entitled “Stem Cells and Their Regenerative Powers,” was held ... Harman, DVM, MPVM was joined by two human doctors: Peter B. Hanson, M.D., Chief ...
(Date:10/10/2017)... ... 10, 2017 , ... The Pittcon Program Committee is pleased ... scientists who have made outstanding contributions to analytical chemistry and applied spectroscopy. Each ... leading conference and exposition for laboratory science, which will be held February 26-March ...
Breaking Biology Technology: