Theoretical and Computational Neuroscience
Author: Guillermina Bruno | email: gbruno@immf.uncor.edu
Guillermina Bruno 1°, Nahir Guadalupe Gazal 2°, Fabián Orlando Ramos 3°, Nahuel Zamponi 4°, Nicolás Unsain 4°
1° 1Laboratorio de Neurobiología, Instituto de Investigación Médica Mercedes y Martín Ferreyra, INIMEC-Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Universidad Nacional de Córdoba (UNC), Córdoba, Argentina
2° Division of Hematology and Oncology, Weill Cornell Medicine, NY, Estados Unidos
The actin/spectrin membrane-associated periodic skeleton (MPS) is a periodic protein structure consisting of actin “rings” located transversely to the axon and separated every 190 nm by α/β-spectrin tetramers “spacers”. In mature neurons, the MPS is organized along almost the entire axonal axis. Little is known about the functionality of this conserved structure. In the present work, public databases and bioinformatics tools were used to elucidate the MPS proteome and interactome, from their fundamental components: actin, 𝛼-spectrin and 𝛽-spectrin. We compared our in silico interactome (protein-protein interaction network, PPI) with recently published immunoprecipitation and mass spectrometry results. We compared the ubiquity of the axonal MPS proteome with proteomes from non-neuronal cells of the three germinal layers. We recognized topological parameters of the PPI network, such as dimensionality, the presence of central nodes, the existence of modules and their correlation with different cellular functions, etc. We also comparatively analyzed PPI networks arising from phylogenetically distant organisms, but in which the MPS has also been found, such as in Caenorhabditis elegans, Drosophila melanogaster, mouse and human. Since proteins do not act alone, performing this type of analysis could provide new insights into the molecular biology of MPS.