Researchers discover secrets of memory-making protein
University of Bergen researchers describe for the first time the structure and stability of a protein implicated in a number of disorders associated with cognitive impairment, such as Alzheimer’s disease, addiction, and neuropsychiatric disorders.
Together with colleagues from University of Bergen (UiB), Centro Nacional de Biotecnologia and University of Grenoble, researcher Craig Myrum of the Department of Biomedicine at the University of Bergen (UiB) has published the article Arc is a flexible modular protein capable of reversible self-oligomerization in the Biochemical Journal, describing the structure of Arc (activity-regulated cytoskeleton associated protein) for the first time.
The study provides new understanding of the Arc protein, which plays a critical role in learning and memory-forming processes. Since the functioning of a protein depends on its three-dimensional structure, learning more about Arc's structure is crucial for further research and understanding of cognitive impairment disorders, such as Alzheimer's disease.
Still a mystery
“Arc expression is required for both the strengthening and weakening of synapses,” says lead author Craig Myrum to Portland Press.
“Thus, it has been described as a ‘master regulator’ of synaptic plasticity and memory-forming processes. However, how Arc does this remains a mystery. Arc appears to be a flexible hub protein capable of interacting with diverse partners in distinct cellular compartments. Our findings may lead to a better understanding of how Arc is regulated at the molecular level,” explains Myrum.
A multidisiplinary approach
Understanding the structure of the protein is essential for the researchers working to develop new therapeutic means of fighting cognitive impairment disorders associated with Arc.
“We are taking a very multidisciplinary approach to learn more about Arc. We are using biochemical assays to uncover novel Arc interaction partners, time-lapse multiphoton microscopy to visualize Arc dynamics, and human genetic analyses to examine whether genetic variation affects Arc-associated processes. We also hope to succeed in more in-depth crystallographic analysis of Arc protein structure,” says Myrum.
Myrum C, Baumann A, Bustad HJ, Flydal MI, Mariaule V, Alvira S, Cuéllar J, Haavik J, Soulé J, Valpuesta JM, Márquez JA, Martinez A, Bramham CR. (2015) Arc is a flexible modular protein capable of reversible self-oligomerization. Biochem J. 468 (145–158) (open access): http://www.biochemj.org/bj/468/bj4680145.htm