Forum for Science, Industry and Business

Sponsored by:     3M 
Search our Site:

 

News from the Mailroom of the Cell - Max Planck Researchers elucidate mechanism of protein

03.09.2014

Cells in an organism communicate with each other via messenger substances. These are often proteins, which after their production inside the cell are transported out of the cell and secreted to the cellular environment. How exactly this export process takes place in detail has remained unclear.

Researchers at the MPI of Biochemistry (MPIB) have now shown in detail how the ‘mailroom of the cell’ sorts a subset of the proteins that are transported out of the cell. “This mechanism regulates the correct sorting of the proteins and is thus essential for the human organism,” said Julia von Blume, research group leader at the MPIB. The results have been published in the Journal of Cell Biology.


Structural model of the human calcium transporter SPCA1: The cofilin binding domain is displayed in purple. The four residues required for direct cofilin binding are indicated as red spheres.

Figure: Dr. Bianca Habermann / Copyright: MPI of Biochemistry

Similarly as we people communicate, our body cells can also exchange brief messages. For this purpose, many of them often use proteins as messengers, such as hormones. These are produced inside the cell and then packed for export in small membrane packages, the vesicles, and sent out from a kind of ‘mailroom’, the so-called Golgi apparatus. But since not all vesicles are destined for export, it is crucial that the proteins are sorted into the correct vesicles. Until now, however, it was unclear how this sorting actually works.

Julia von Blume and her team of the research group “Molecular Basis of Protein Trafficking” at the MPIB are dedicated to finding the answer to this question. In previous studies they showed that the interaction of three proteins is decisive for the sorting process. Actin, a central support and transport molecule, and cofilin, a protein complex, work together. Near the vesicles they bind the calcium transporter SPCA1, which increases the local concentration of calcium. That attracts the corresponding proteins, which are then incorporated into a vesicle and exported from the cell.

In the current publication, the scientists elucidated the specific molecular mechanism underlying these steps. By investigating the individual proteins in isolation as well as in living cells, they were able to precisely decipher their interaction (down to the amino acids).

The new findings not only confirm the previous studies, but are also medically relevant: “This mechanism regulates the correct sorting of the proteins in the Golgi apparatus and is thus essential for the human organism,” said Julia von Blume, illustrating her explanation with an example: “If this process is impaired, severe health problems such as the skin disease Hailey-Hailey can be the result. It is assumed that due to a genetic defect, the calcium transporter SPCA1 does not function and therefore certain proteins that are important for cell-cell communication in the epidermis can no longer be exported from the cell.“ Patients with Hailey-Hailey disease thus suffer from discoloration of the skin, itching and blisters.

In the future, the scientists hope to clarify whether other proteins are involved in the process – always with the objective to ultimately reconstruct the entire process.
[HS]

Original publication:
C. Kienzle, N. Basnet, A. Crevenna, G. Beck, B. Habermann, N. Mizuno and J. von Blume: Cofilin recruits F-actin to SPCA1 and promotes Ca2+-mediated secretory cargo sorting. Journal of Cell Biology, September 1, 2014.
DOI: 10.1083/jcb.201311052

Contact:
Dr. Julia von Blume
Molecular Basis of Protein Trafficking
Max Planck Institute of Biochemistry
Am Klopferspitz 18
82152 Martinsried
Germany
e-mail: vonblume@biochem.mpg.de
http://www.biochem.mpg.de/blume

Anja Konschak
Public Relations
Max Planck Institute of Biochemistry
Am Klopferspitz 18
82152 Martinsried
Germany
Phone: +49 89 8578-2824
e-mail: konschak@biochem.mpg.de
http://www.biochem.mpg.de

Weitere Informationen:

http://www.biochem.mpg.de/blume
http://Website of the Research Group “Molecular Basis of Protein Trafficking” (Julia von Blume)

Anja Konschak | Max-Planck-Institut

Further reports about: Biochemistry Biology Cell Klopferspitz MPIB Max-Planck-Institut Molecular Protein mechanism organism proteins vesicles

More articles from Life Sciences:

nachricht Toward a 'smart' patch that automatically delivers insulin when needed
18.01.2017 | American Chemical Society

nachricht 127 at one blow...
18.01.2017 | Stiftung Zoologisches Forschungsmuseum Alexander Koenig, Leibniz-Institut für Biodiversität der Tiere

All articles from Life Sciences >>>

The most recent press releases about innovation >>>

Die letzten 5 Focus-News des innovations-reports im Überblick:

Im Focus: How gut bacteria can make us ill

HZI researchers decipher infection mechanisms of Yersinia and immune responses of the host

Yersiniae cause severe intestinal infections. Studies using Yersinia pseudotuberculosis as a model organism aim to elucidate the infection mechanisms of these...

Im Focus: Interfacial Superconductivity: Magnetic and superconducting order revealed simultaneously

Researchers from the University of Hamburg in Germany, in collaboration with colleagues from the University of Aarhus in Denmark, have synthesized a new superconducting material by growing a few layers of an antiferromagnetic transition-metal chalcogenide on a bismuth-based topological insulator, both being non-superconducting materials.

While superconductivity and magnetism are generally believed to be mutually exclusive, surprisingly, in this new material, superconducting correlations...

Im Focus: Studying fundamental particles in materials

Laser-driving of semimetals allows creating novel quasiparticle states within condensed matter systems and switching between different states on ultrafast time scales

Studying properties of fundamental particles in condensed matter systems is a promising approach to quantum field theory. Quasiparticles offer the opportunity...

Im Focus: Designing Architecture with Solar Building Envelopes

Among the general public, solar thermal energy is currently associated with dark blue, rectangular collectors on building roofs. Technologies are needed for aesthetically high quality architecture which offer the architect more room for manoeuvre when it comes to low- and plus-energy buildings. With the “ArKol” project, researchers at Fraunhofer ISE together with partners are currently developing two façade collectors for solar thermal energy generation, which permit a high degree of design flexibility: a strip collector for opaque façade sections and a solar thermal blind for transparent sections. The current state of the two developments will be presented at the BAU 2017 trade fair.

As part of the “ArKol – development of architecturally highly integrated façade collectors with heat pipes” project, Fraunhofer ISE together with its partners...

Im Focus: How to inflate a hardened concrete shell with a weight of 80 t

At TU Wien, an alternative for resource intensive formwork for the construction of concrete domes was developed. It is now used in a test dome for the Austrian Federal Railways Infrastructure (ÖBB Infrastruktur).

Concrete shells are efficient structures, but not very resource efficient. The formwork for the construction of concrete domes alone requires a high amount of...

All Focus news of the innovation-report >>>

Anzeige

Anzeige

Event News

12V, 48V, high-voltage – trends in E/E automotive architecture

10.01.2017 | Event News

2nd Conference on Non-Textual Information on 10 and 11 May 2017 in Hannover

09.01.2017 | Event News

Nothing will happen without batteries making it happen!

05.01.2017 | Event News

 
Latest News

A big nano boost for solar cells

18.01.2017 | Power and Electrical Engineering

Glass's off-kilter harmonies

18.01.2017 | Materials Sciences

Toward a 'smart' patch that automatically delivers insulin when needed

18.01.2017 | Life Sciences

VideoLinks
B2B-VideoLinks
More VideoLinks >>>