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New understanding of protein's role in brain

Date:
April 13, 2010
Source:
McGill University
Summary:
Brains in mammals modify a particular protein in a unique way, which alters the protein's normal function according to new research. The modified protein plays a key role in memory processes. This discovery represents an important step in understanding how our brains work.
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How do we process thoughts and store memories? A team of researchers headed by Dr. Nahum Sonenberg of McGill's Department of Biochemistry and Goodman Cancer Centre has discovered that brains in mammals modify a particular protein in a unique way, which alters the protein's normal function. This discovery represents an important step in understanding how our brains work.

When our memories are being formed, nerve cells, or neurons, communicate with each other through electrical impulses at specialized connections. To strengthen these connections, the neurons require new proteins -- key molecules needed for all forms of cellular activity. The protein in question, 4E-BP2, controls the process of producing new proteins in the nervous system.

This process, known as protein synthesis or translation, is the major focus of research in Sonenberg's laboratory. Before the team's discovery, no one knew 4E-BP2 could be chemically altered in such a manner as the team described in its work, much less that this could have an effect on neuron function.

According to the lead researcher Dr. Michael Bidinosti, a recent graduate from Sonenberg's laboratory, "we found a modification to a protein that controls the cellular protein-synthesis machinery. This modification seems to affect the ability of nerve cells to communicate with each other and is thought to be part of the processes underlying memory."

He explains that study of protein synthesis and of memory are increasingly converging fields, and that the team's research is an important achievement in this arena. Collaboration was critical to the discovery as the team includes researchers from the Université de Montréal, the Montreal Neurological Institute, the University of Toronto, Baylor College of Medicine in Houston, and the University of Bergen in Norway.

"Better understanding of protein synthesis in the brain is crucial to the advancement of neuroscience, particularly as researchers discover that altered proteins may have a direct impact on the memory process," says Dr. Anthony Phillips, Scientific Director of the Canadian Institutes of Health Research (CIHR) Institute of Neurosciences, Mental Health and Addiction. "CIHR hopes that these new findings will lead to more research aimed at ultimately solving memory loss issues."

The research was published in the journal Molecular Cell on March 25, 2010, and was funded by the Canadian Institutes of Health Research and the Howard Hughes Medical Institute. Bidinosti was supported by a Postgraduate Doctoral Scholarship from the Natural Sciences and Engineering Research Council of Canada (NSERC).


Story Source:

The above post is reprinted from materials provided by McGill University. Note: Materials may be edited for content and length.


Journal Reference:

  1. Michael Bidinosti, Israeli Ran, Maria R. Sanchez-Carbente, Yvan Martineau, Anne-Claude Gingras, Christos Gkogkas, Brian Raught, Clive R. Bramham, Wayne S. Sossin, Mauro Costa-Mattioli et al. Postnatal Deamidation of 4E-BP2 in Brain Enhances Its Association with Raptor and Alters Kinetics of Excitatory Synaptic Transmission. Molecular Cell, 26 March 2010; 37(6) pp. 797 - 808 DOI: 10.1016/j.molcel.2010.02.022

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McGill University. "New understanding of protein's role in brain." ScienceDaily. ScienceDaily, 13 April 2010. <www.sciencedaily.com/releases/2010/03/100325131553.htm>.
McGill University. (2010, April 13). New understanding of protein's role in brain. ScienceDaily. Retrieved July 27, 2015 from www.sciencedaily.com/releases/2010/03/100325131553.htm
McGill University. "New understanding of protein's role in brain." ScienceDaily. www.sciencedaily.com/releases/2010/03/100325131553.htm (accessed July 27, 2015).

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